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Blood

Blood – BIOCHEMISTRY

Compiled Topical Questions of Blood – Biochemistry

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If you were the body’s iron gatekeeper, you’d need a hormone that decides when to lock or unlock the iron export door.

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Tags: 2024

Which of the following proteins in blood plasma regulates the release of iron from the intestine, liver, and bone marrow?

When you need to pull oxygen across the placenta from mom’s blood, would tighter or looser hemoglobin binding help more?

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Tags: 2024

As compared to HbA, HbF has which of the following characteristics?

When one side of glycolysis skips a payday, the total profit takes a hit—but doesn’t vanish.

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Tags: 2024

During glycolysis, 1 molecule of glucose is metabolized into 2 molecules of glyceraldehyde-3-phosphate (G3P). If one G3P molecule undergoes the Rapoport-Luebering shunt (bypassing ATP generation at phosphoglycerate kinase), while the other proceeds through normal glycolysis, what is the net ATP yield from the complete glycolysis of that one glucose molecule?

Consider which vitamin improves the body’s ability to absorb plant-based sources of iron, especially in vegetarian diets.

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Which of the following vitamins helps in the absorption of non-heme iron in the gastrointestinal tract?

When the body wants to hold on to oxygen more tightly, ask yourself — under what conditions would hemoglobin become extra clingy?

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Tags: 2022

Which of the following changes shifts the oxygen dissociation curve to the left?

Consider where the cell’s powerhouse might double as a workshop for building both energy and iron-containing structures.

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The first step of heme synthesis takes place in which part of the cell?

Think about what’s deliberately left out when serum is separated from blood — especially something that would normally help a clot form, but isn’t needed in a fluid meant for analysis.

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Tags: 2022

When a serum sample is electrophoresed, which of the following band is normally absent?

Consider the role of each plasma protein and where they might migrate on electrophoresis based on their size and charge. Which proteins are directly involved in immune defense?

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Tags: 2023

The plasma proteins electrophoresis shows two major protein electrophoretic bands, one for albumin and the other for globulin. Globulin further gives different fractions. These are α1 globulins, α2 globulin, β1 globulin, β2 globulin, and γ globulins. Which of the following is the protein present in the γ globulin fraction?

Enzymes that modify proteins for critical functions—like coagulation—often rely on coenzymes in their reduced form. What happens if that reduction-oxidation cycle is blocked?

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Tags: 2023

Which form of vitamin K is required for the activation of clotting factors?

If a cell has no mitochondria, what energy pathway does it rely on—and how efficient is it compared to oxidative phosphorylation?

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Tags: 2023

What is the net yield of ATP molecules produced by the glycolysis of one glucose molecule in red blood cells?

If a molecule changes color from green to yellow during degradation, consider which compound might come first and what enzyme is involved in that color transformation.

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Tags: 2023

Which of the following is the first bile pigment produced in the catabolism of heme molecule?

Think about what happens when your body’s oxygen delivery can’t keep up with demand. What compensatory energy pathway kicks in — and what byproduct builds up quickly?

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Tags: 2023

Elevated concentration of lactate in the plasma is associated with which of the following?

Think about the protein that protects the body from oxidative damage by capturing free hemoglobin immediately after RBC destruction.

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Tags: 2021

Which protein does hemoglobin bind to after hemolysis of red blood cells?

 

Which vitamin is essential for the building blocks of DNA, thus affecting rapidly dividing cells like those producing red blood cells?

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Tags: 2021

Which vitamin deficiency causes anemia?

Which enzyme’s name literally describes the act of “inserting iron” into a ring structure, and ends the heme production line?

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Tags: 2021

In heme synthesis, Fe2+ is added to protoporphyrin to form heme. Which enzyme is needed for this process?

In the final step of heme synthesis, which enzyme is responsible for inserting iron into protoporphyrin, and what happens when this step fails?

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Tags: 2021

Deficiency of which of the following enzymes causes protoporphyria?

 

Which intracellular protein safely holds iron in a readily usable form, releasing it when iron is scarce but storing it securely when abundant?

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Tags: 2021

Which protein shows the highest storage reserves of iron?

Which molecule added to bilirubin in the liver makes it water-soluble and ready for excretion?

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Tags: 2021

Which of the following is attached to unconjugated bilirubin to form conjugated bilirubin?

Which syndrome results from a complete absence of the enzyme responsible for conjugating bilirubin, leading to dangerous levels of unconjugated bilirubin?

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Tags: 2021

Complete lack of glucuronidation results in which of the following diseases?

when deficient, leads to accumulation of photosensitive intermediates?

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Tags: 2021

The deficiency of which of the following enzymes causes erythropoietic protoporphyria?

Which plasma protein specifically binds iron ions to transport them safely and deliver them where needed, while preventing free iron from causing damage?

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Tags: 2021

What of the following is the iron transporter protein in the plasma?

Which vitamin’s active forms are crucial cofactors in amino acid metabolism ?

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Tags: 2021

Pyridoxamine, pyridoxine, and pyridoxal are forms of which vitamin?

Consider the globin chains that dominate after birth and throughout adult life, responsible for efficient oxygen delivery in tissues.

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Tags: 2021

Which chains are involved in the formation of hemoglobin A?

Which protein is so essential to the vascular system that a drop in its levels causes fluid to leak out of capillaries, and is also tasked with shuttling many molecules through the bloodstream?

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Tags: 2021

Which protein plays a major role in maintaining oncotic pressure and transportation of lipids and steroids?

To function in DNA synthesis and repair, folic acid must undergo enzymatic changes. What form do you think acts as the “working hands” of folate, helping transfer one-carbon units during biosynthetic reactions?

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Tags: 2022

Which of the following options is the functionally active form of folic acid?

When analyzing the name of a compound, consider if it subtly hints at any of its molecular components. Which element might lie at the core of a structure whose name sounds like it includes part of the periodic table?

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Tags: 2022

The corrin ring in cobalamin(vitamin B12), is bound to which of the following trace elements?

In disorders where sunlight causes the skin to blister, consider the accumulation of light-sensitive intermediates. Which enzymatic block would cause these intermediates to build up in the skin rather than progressing smoothly down the biosynthetic pathway?

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Tags: 2022

A 7-year-old boy developed vesicles and bullae on his face and arms due to prolonged sun exposure from participating in sports activities. His father had a similar condition. He is suspected of porphyria cutanea tarda. Which of the following enzymes is mainly deficient in the above-mentioned disease condition?

When considering coenzymes, think about reactions involving amino acids. What kind of enzymatic activity typically demands a coenzyme derived from vitamin B6?

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Tags: 2022

Which of the following enzymes in the heme biosynthesis pathway requires pyridoxal phosphate as a coenzyme?

Think about what happens when a polar, negatively charged residue is replaced with a non-polar one in a protein that has to stay soluble under oxygenated conditions. What kind of substitution could make the molecule stick to others and form polymers under low oxygen?

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Tags: 2022

In hemoglobin S (HbS), which amino acid residue is substituted by valine at the sixth position of the beta-globin chain?

When red cells break apart, something needs to “rescue” the valuable iron from escaping into the kidneys and making the urine red. What acts as this emergency escort in the bloodstream?

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Tags: 2022

Extracellular hemoglobin is bound to a plasma protein in order to avoid loss of hemoglobin in urine. Which plasma protein binds free hemoglobin?

Think about which substrate originates from the TCA cycle, and which is a non-essential amino acid involved in nitrogen donation. The product of their union will set off a chain of porphyrin reactions.

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Tags: 2022

What are the substrates of heme synthesis?

Consider which cofactor is required to unlock the potential of the other in order to contribute to the complex task of nucleotide synthesis. The conversion step is the key to cellular replication.

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Tags: 2022

Which of the following statement is correct regarding folic acid and vitamin B12?

In a multi-step pathway where each reaction relies on a catalyst, what happens if just one of those catalysts fails — what does that turn the entire assembly line into?

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Tags: 2020

Porphyria results in the accumulation of a unique pattern of intermediates caused by the deficiency of which of the following?

When red blood cells rupture in the bloodstream, hemoglobin is released freely. This free hemoglobin is toxic and must be quickly sequestered. Ask yourself: which plasma protein acts as a first responder, binding hemoglobin in the circulating blood, not just transporting its breakdown products?

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Tags: 2023

After the breakdown of red blood cells, which of the following proteins binds hemoglobin to be cleared by liver macrophages?

This minor hemoglobin component typically makes up only a few percent of the total but becomes important in diagnosing certain thalassemias.

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Tags: 2023

Which one of the following values corresponds to the percentage of hemoglobin A2 (HbA₂) in a normal adult person?

Some proteins surge dramatically in response to tissue injury or infection—consider which group behaves like emergency first responders in the bloodstream, rather than steady-state carriers or enzymes.

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Tags: 2023

C-reactive protein, which is elevated in case of inflammation and infection, falls into the category of which of the following plasma proteins?

Think about the enzyme that cracks open a toxic ring structure in old red cells — the first to act before any pigments or color changes appear.

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Tags: 2020

In reticuloendothelial cells, what initially degrades heme?

These signaling molecules are synthesized by ribosomes and folded into specific 3D structures to fit receptors precisely — what kind of macromolecules follow that script?

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Tags: 2020

What are growth factors usually made of?

This reaction marks the gateway to synthesizing an iron-binding molecule essential for oxygen transport and cellular respiration. Consider which enzyme initiates the path that eventually leads to hemoglobin formation.

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Tags: 2020

Glycine and succinyl CoA combine to form delta-aminolevulinic acid in the presence of which enzyme?

When thinking about this enzyme, focus on what the cell gains from this reaction — especially in tissues that rely on antioxidant defense. Consider how red blood cells, without mitochondria, manage oxidative stress.

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Tags: 2020

What does glucose-6-phosphate dehydrogenase do?

When a build-up of photosensitive intermediates causes skin fragility, consider which step removes carboxyl groups from the tetrapyrrole precursors—and what happens if that step stalls.

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Tags: 2023

A 7-year-old boy developed vesicles and bullae on his face and arms due to prolonged sun exposure from participating in sports activities. His father had a similar condition. He is suspected of porphyria cutanea tarda. Which of the following enzymes is mainly deficient in the above-mentioned disease condition?

Imagine the very first enzyme in the pathway grabbing two small molecules—one from the Krebs cycle and one an amino acid—to build the foundational ring of heme.

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Tags: 2023

Which of the following components are involved in the first step of heme synthesis?

Reflect on a disorder where hemoglobin is present but cannot carry oxygen effectively due to changes in the chemical state of iron — what oxidation state change would explain this impaired function?

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Tags: 2022

In which of the following conditions does iron undergo oxidation from ferrous to the ferric form in hemoglobin?

Think about how nutrients are stored in foods versus how they are absorbed in the intestine. What form might a vitamin take to stay stable in foods but need to be modified before entering the bloodstream?

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Tags: 2022

In which of the following forms is dietary folate present?

This vitamin is often deficient in strict vegans and plays a crucial role in both DNA synthesis and neurological function. Its absence traps folate in an unusable form, indirectly leading to megaloblastic anemia. Consider the coenzymes needed in methylation cycles.

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Tags: 2022

Which vitamin is required for the conversion of 5-methyl-tetrahydrofolate to tetrahydrofolate in the conversion of homocysteine to methionine?

Which disorder is caused by a change in the primary structure of hemoglobin that alters its solubility and leads to a drastic change in red blood cell shape, especially under low oxygen tension?

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Tags: 2022

Which disease occurs when the hydrophilic amino acid glutamic acid is replaced by the hydrophobic amino acid valine at position 6 in the globin chain?

In metabolic disorders, consider whether symptoms involve the nervous system, the skin, or both. Which clinical patterns tend to arise when an intermediate in the heme synthesis pathway accumulates in tissues exposed to light?

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Tags: 2021

Which of the following results from the deficiency of uroporphyrinogen decarboxylase?

Consider which substrates are derived from both the TCA cycle and amino acid metabolism, and how they might contribute to the formation of a porphyrin ring structure.

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Tags: 2021

Which of the following components are involved in the first step of heme synthesis?

Which protein is involved in the clotting process, and because it’s used up when a clot forms, it’s absent in serum but still present in plasma? Consider which option plays a role in the transition from liquid blood to a solid clot.

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Tags: 2022

What protein is found in plasma, but not in serum, and can appear as a distinct band on electrophoresis that may sometimes be confused with multiple myeloma?

In the adult hemoglobin profile, there’s one form that makes up a very small fraction but becomes diagnostically important in disorders like β-thalassemia. It’s not the major form, but it quietly plays a big role in screening tests. What percentage would you expect for such a minor component?

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Tags: 2022

Which of the following corresponds to the percentage of HbA2 in adults?

When vitamins are converted into coenzymes, consider which form serves as the core scaffold that carries functional groups in various biochemical pathways—especially in DNA and amino acid synthesis.

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Tags: 2022

Which of the following options is the functionally active form of folic acid?

Think about how the body makes fat-soluble substances easier to excrete through bile and urine. What type of biochemical group does the liver commonly add to such molecules to enhance their water solubility?

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Tags: 2020

Hemoglobin is broken down into heme and globin followed by the conversion of biliverdin into bilirubin. Inside the hepatic system, what does bilirubin gets conjugated with?

Consider not just which proteins can interact with copper, but which one serves as the body’s dedicated carrier and regulator of copper. Which one would be affected in a disease where copper builds up?

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Tags: 2020

Which of the following is the most important copper-containing protein?

Think about how trace metal-dependent proteins often act as intermediaries in metabolic transitions. Which type of transformation involving metal ions might be critical for enabling systemic transport through specific carrier proteins?

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Tags: 2020

Which of the following regarding ceruloplasmin is correct?

This protein is involved in the storage of iron within cells and is released into the bloodstream when the body needs to regulate iron levels.

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Tags: 2021

Most of the iron in the storage pool is in the form of which of the following?

The adult hemoglobin molecule achieves function through a balanced pairing of two types of globin chains. Reflect on the basic structural symmetry of hemoglobin and the predominant chains expressed after birth.

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Tags: 2019

What is the composition of hemoglobin A or HbA1?

Think about conditions where chronic blood glucose levels matter more than single-point readings, and how long-living proteins can act as record-keepers of such levels. Which disease would require this kind of ongoing metabolic tracking?

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Tags: 2019

Hemoglobin A1c (HbA1C) levels are used in the identification of which of the following diseases?

Which protein acts like your bloodstream’s multitasker—holding water in, carrying hormones around, and keeping the pressure balanced?

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Tags: 2020

Which of the following is the most abundant plasma protein?
 

Think about which form of a coenzyme would be required to assist with mitochondrial reactions involving rearrangement of carbon skeletons, such as converting methylmalonyl-CoA to succinyl-CoA.

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Tags: 2020

What is the major form of vitamin B12 found in human tissue and mitochondria?

Focus on the role of the delta chain in the context of β-thalassemia. What happens when there is a reduced production of beta-globin chains, and how does the body compensate?

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Tags: 2020

A pathologist examines a hemoglobin electrophoresis slide of a patient suffering from beta-thalassemia trait. Which hemoglobin will most likely be seen?

Which vitamin acts as a powerful antioxidant and plays a direct role in electron transfer and redox reactions involving iron?

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Tags: 2020

Which of these results in the reduction of the formation of methemoglobin from hemoglobin?

Which chronic condition is best monitored by tracking how much sugar is permanently attached to hemoglobin over time, rather than just looking at current blood sugar levels?

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Tags: 2020

Glycosylated hemoglobin test (HbA1C) levels can be measured to diagnose which of the following?

Focus on the substance that binds to bilirubin to increase its water solubility, enabling it to be excreted in bile. Don’t confuse the enzyme that catalyzes this reaction with the actual compound that conjugates with bilirubin.

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Tags: 2019

Bilirubin is conjugated with which of the following?

Think about a protein that plays a key role in redox reactions involving metal ions and whose deficiency can lead to a condition involving copper accumulation in tissues.

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Tags: 2019

Ceruloplasmin transports which of the following?

Which negatively charged amino acid, when replaced by a hydrophobic one in the beta-globin chain, disrupts the normal solubility and leads to hemoglobin polymerization under hypoxia?

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Tags: 2020

In hemoglobin S (HbS), which amino acid residue is substituted by valine at the sixth position of the beta-globin chain?

Think of the heme group as a cyclic scaffold that holds iron—how many basic nitrogen-containing ring structures form this scaffold?

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Tags: 2020

How many pyrrole rings are present in one molecule of hemoglobin?

Which vitamin contains cobalt and is critical for both DNA synthesis and neurologic function, particularly in preventing megaloblastic anemia?

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Tags: 2020

What is the other name for cobalamin?

When constructing a powerful biological pigment, which enzyme plays the finishing role—placing the critical metal ion into its ring structure, turning an inert molecule into a functional powerhouse?

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Tags: 2020

In the formation of hemoglobin, which enzyme is involved in the incorporation of Fe into protoporphyrin IX?

In HbC, the mutation introduces a residue with the opposite charge of the one it replaces—how might that affect the molecule’s interaction with its environment compared to sickle cell hemoglobin?

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Tags: 2020

In hemoglobin C (HbC), which amino acid is substituted for glutamate?

In HbC, the mutation introduces a residue with the opposite charge of the one it replaces—how might that affect the molecule’s interaction with its environment compared to sickle cell hemoglobin?

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Tags: 2020

In hemoglobin C (HbC), which amino acid is substituted for glutamate?

This porphyria blisters under the sun and stains your urine like old tea, all thanks to one lazy decarboxylase.

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Tags: 2018

In which disease is uroporphyrinogen decarboxylase deficient?

Which enzyme begins the entire heme synthesis journey and decides whether or not the cell commits to the process, especially when iron and erythropoietin knock at the door?

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Tags: 2018

Heme synthesis in erythroid tissue is regulated by which of the following enzymes?

The pathway starts with an amino acid and a citric acid cycle intermediate — one comes from protein, the other from metabolism. Together, they launch the synthesis of life’s iron-binding pigment.

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Tags: 2018

What are the substrates of heme synthesis?

Which vitamin donates the essential building blocks for two major DNA bases, without which your cells couldn’t divide?

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Tags: 2018

Regarding folic acid and vitamin B12 function in DNA synthesis, which of the following is correct?

There’s a brief embryonic cast with more ancient names—think of the earliest duo formed in the yolk sac, long before birth.

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Tags: 2018

Which of these is the correct composition of hemoglobin Gower 1?

Consider how a tiny genetic typo—swapping just one building block—can ripple into a structural crisis, especially in a protein designed to carry life’s most vital gas.

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Tags: 2020

What causes sickle cell disease?

Think about the enzyme that opens up the heme ring and releases carbon monoxide — a rare example of a gas generated in normal human metabolism.

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Tags: 2019

What enzyme catalyzes the first step of heme degradation?

Think about the series of steps in any biochemical pathway. When one enzyme is deficient, it can block the pathway at a specific point, leading to the accumulation of toxic intermediates. Consider which molecules in the heme pathway are typically found in excess.

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Tags: 2019

Porphyria results in the accumulation of a unique pattern of intermediates caused by the deficiency of which of the following?

Sometimes a cofactor isn’t the main actor in the process—but it holds the key to letting the star performer function. Think about which of these vitamins acts as the unlocker, allowing the other to actively contribute to DNA synthesis.

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Tags: 2019

Which of the following statement is correct regarding folic acid and vitamin B12?

Among these options, consider which food group is known for containing a compound that helps unlock iron’s solubility and makes it easier for your gut to take it in.

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Tags: 2019

Which of the following foods cause the best iron absorption in the gut?

Consider how your body deals with iron in its less absorbable forms. What dietary substance might chemically assist in converting iron into a more usable state while also protecting it from forming insoluble compounds?

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Tags: 2019

A patient is given oral iron supplements. Which of the following in the diet would increase iron absorption in the gut?

Think about how fetal red cells adapt to life in a low-oxygen environment. What structural adjustment in hemoglobin allows the fetus to draw oxygen more effectively from maternal circulation?

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Tags: 2018

What is the composition of HbF?

When diagnosing a type of anemia caused by impaired DNA synthesis, what two nutrients are crucial for proper red blood cell production, and how can their deficiencies be confirmed?

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Tags: 2019

Which diagnostic test is done for megaloblastic anemia?

Which type of hemoglobin lacks beta chains and therefore avoids the very polymerization process that leads to the sickling of red blood cells?

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Tags: 2019

In sickle cell anemia, which type of hemoglobin is most useful?

This mutation swaps a water-loving residue with one that shuns water, introducing a “sticky” patch on the hemoglobin molecule — and that subtle change sets off a cascade of structural consequences. Consider the polarity of the amino acids involved.

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Tags: 2019

In sickle cell anemia, glutamate at the sixth position of the beta chain of hemoglobin is substituted by which of the following amino acids?

At what age does the body begin relying heavily on beta-globin chains, making conditions that affect their production become symptomatic?

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Tags: 2019

How long after birth does the transition from HbF to HbA take place in patients with thalassemia major?

Which hemoglobin is made from the most primitive forms of both the alpha-like and beta-like globin chains, present only in the earliest stages of life before the liver and bone marrow take over?

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Tags: 2019

Which of these is the correct composition of hemoglobin Gower 1?

Consider what might happen in a multi-step pathway if one of the steps is slowed down or blocked—not by an external substance, but because a key worker in the chain is missing or dysfunctional.

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Tags: 2019

In porphyrias, which of the following factors is involved?

When thinking about vitamins related to DNA synthesis and the production of red blood cells, consider which one assists in the recycling and activation of folate.

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Tags: 2019

Which of the following vitamins is related to the metabolism of folic acid?

Think about the hemoglobin form that takes over after birth and stays dominant for life. It balances two chains that come from different globin gene clusters.

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Tags: 2018

What is the composition of hemoglobin A or HbA1?

Despite being stored in the liver and required in small amounts, this vitamin’s deficiency can lead to severe neurological and hematological effects. Consider how tightly regulated the daily intake needs to be.

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Tags: 2019

What is the daily requirement for Vitamin B12?

Which vitamin is essential for enabling clotting factors to bind calcium and function, and is also antagonized by warfarin?

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Tags: 2017

Which of the following vitamins do the clotting factors II, VII, IX, and X depend on for their synthesis?

Which enzyme class adds a specific chemical group to help coagulation factors stick to calcium — a step that’s absolutely dependent on vitamin K?

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Tags: 2017

Which one of the following enzymes is dependent on vitamin K to help in the formation of coagulation factors?

Understanding protein function often requires looking at their structure. In hemoglobin, each chain’s size is carefully balanced for cooperative oxygen binding. Consider the relative lengths of the different globin chains — which might be shorter or longer, and why?

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Tags: 2017

How many amino acids does alpha-hemoglobin have?

Consider the foundational building blocks of heme. One comes from a metabolic intermediate related to energy production, while the other is an amino acid. Which two substances work together to create the core structure of heme

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Tags: 2017

What is pyrrole made up of?

Consider the enzymatic pathways that diverge once arachidonic acid is freed from the membrane. Different enzymes give rise to distinct families of signaling molecules, each with their own roles in inflammation and homeostasis. Which pathway leads to mediators known for attracting leukocytes and tightening airways?

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Tags: 2017

Leukotrienes are synthesized by which of the following?

Consider how the body handles this compound: it’s stored efficiently, absorbed with the help of intrinsic factors, and can take years to deplete. When something is that conserved and potent, would the daily need be large or minimal?

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Tags: 2017

What is the daily requirement for Vitamin B12?

Think about how the body protects the kidneys from iron-containing proteins when red cells rupture in circulation. What “scavenger” protein quickly binds to free-floating heme before it causes oxidative damage or is lost in urine?

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Tags: 2018

Extracellular hemoglobin is bound to a plasma protein in order to avoid loss of hemoglobin in urine. Which plasma protein binds free hemoglobin?

Think about which protein the liver produces in large amounts that has no sugar attached, yet plays a key role in holding fluid inside blood vessels—especially relevant in edema and malnutrition.

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Tags: 2018

Which unglycosylated protein affects the osmotic pressure of human plasma?

Think about how a single swap—from a water-loving to a water-avoiding amino acid—can twist a flexible, round traveler into a stiff, crescent-shaped saboteur.

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Tags: 2018

In sickle cell anemia, glutamate at the sixth position of the beta chain of hemoglobin is substituted by which of the following amino acids?

Which hemoglobin combination dominates before you’re even born—equipping you with oxygen-grabbing power that fades after your first breath?

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Tags: 2016

What is the composition of hemoglobin F (HbF)?

Imagine trying to absorb nutrients that dissolve in oil, but suddenly, your body can’t release the digestive fluid that breaks down fats. Which group of nutrients would you struggle to absorb—and which one of them is essential to stopping a cut from bleeding?

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Tags: 2017

Obstructive jaundice leads to the deficiency of:

Among all plasma proteins, consider which one not only dominates in quantity but also plays a role in stabilizing the circulatory environment — from osmotic balance to transport — across almost every system in the body.

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Tags: 2017

Which of the following is a major plasma protein?

Think about which amino acid change causes red blood cells to turn from flexible discs into rigid, sickle-shaped forms. Which specific codon alteration leads to the formation of hemoglobin S instead of hemoglobin A?

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Tags: 2016

Which one of the following base-pair change is the cause of sickle cell anemia?

Consider which organ is best equipped not just to initiate a transformation, but to manage and process byproducts for safe removal from the body. Think about the body’s waste management strategy for substances derived from essential but potentially toxic molecules.

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Tags: 2017

Heme is broken down in which of the following?

When cellular components are dismantled, each part follows a distinct biochemical fate. Think about which segment of the hemoglobin molecule is not made of protein and contains an essential metal, and consider what becomes of that structure when the cell is no longer viable.

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Tags: 2017

The breakdown of heme produces which of the following?

Think about the hemoglobin that dominates after birth and becomes the oxygen ferry for the rest of your adult life. Which globin chains pair up to do this job most of your life?

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Tags: 2016

What is the composition of hemoglobin A (HbA)?

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