Biochemistry of Blood
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Questions and Answers

What are the primary components of haemoglobin?

Haemoglobin is composed of haem and globin.

Explain the coordination bonds present in haem.

Haem has two additional coordination bonds: the 5th bond links to proximal histidine, and the 6th bond is linked to oxygen in oxyhemoglobin.

What is the structural difference between the α chains and β chains of adult Hb?

The α chains consist of 141 amino acids, while the β chains contain 146 amino acids.

What type of porphyrin is biologically significant in haem and cytocromes?

<p>The biologically important porphyrin found in haem and cytochromes is Type III isomer.</p> Signup and view all the answers

How does haemoglobin protect iron from oxidation?

<p>Haemoglobin provides an environment that allows the binding of oxygen while blocking the final step of oxidation.</p> Signup and view all the answers

What is the primary type of adult hemoglobin and its composition?

<p>The primary type of adult hemoglobin is HbA, which is composed of two alpha and two beta chains (α2β2).</p> Signup and view all the answers

Describe the composition of a haem molecule.

<p>A haem molecule contains iron and a porphyrin ring derived from four pyrrole rings.</p> Signup and view all the answers

What role do side chains play in the structure of porphyrins?

<p>Side chains in porphyrins are substituted for hydrogen atoms and define the characteristics of different porphyrin types.</p> Signup and view all the answers

What is the primary defect in α-Thalassemia?

<p>The primary defect is a decreased or absent synthesis of α chains of hemoglobin.</p> Signup and view all the answers

What types of chains are produced in HbH disease?

<p>In HbH disease, there are four β chains produced.</p> Signup and view all the answers

Describe the main difference between congenital and acquired Met Hemoglobinemia.

<p>Congenital Met Hemoglobinemia is due to genetic mutations, while acquired arises from exposure to drugs or toxins.</p> Signup and view all the answers

Which type of hemoglobin is primarily produced in β-Thalassemia?

<p>Excess HbA2 (α2δ2) and HbF (α2γ2) are primarily produced.</p> Signup and view all the answers

What is the characteristic blood color observed in patients with Methemoglobinemia?

<p>The blood appears brownish in color.</p> Signup and view all the answers

What diagnostic test can be used to measure oxygen saturation in Methemoglobinemia?

<p>Pulse oximetry can be used to test the saturation of blood oxygen.</p> Signup and view all the answers

What treatment is usually ineffective for congenital Hemoglobin M?

<p>Treatment with reducing agents like methylene blue is ineffective.</p> Signup and view all the answers

Name two causes of acquired Met Hemoglobinemia.

<p>Ingestion of large amounts of phenacetin or exposure to excess nitrites are causes.</p> Signup and view all the answers

What chains make up Minor Adult Hemoglobin (Hb A₂)?

<p>Two Alpha chains and two Delta chains.</p> Signup and view all the answers

How does the glycosylation of hemoglobin occur in Glycosylated Hb (Hb A₁C)?

<p>It occurs through a non-enzymatic reaction where glucose is linked to the e-amino group of lysine.</p> Signup and view all the answers

Describe the primary component chains of Fetal Hemoglobin (HbF).

<p>Fetal Hemoglobin consists of two Alpha chains and two Gamma chains.</p> Signup and view all the answers

What mutation leads to Sickle Cell Disease (HbS)?

<p>A mutation replacing Glutamic acid with Valine at the 6th position of the Beta chain.</p> Signup and view all the answers

What are the consequences of sickle-shaped red blood cells? List two effects.

<p>They are fragile, leading to anemia, and can get trapped in small blood vessels, causing thrombus formation.</p> Signup and view all the answers

What is a normal reticulocyte count in sickle cell disease diagnosis?

<p>A normal reticulocyte count is between 10-20%.</p> Signup and view all the answers

How does electrophoresis help in the diagnosis of Sickle Cell Disease?

<p>It shows the presence of HbS and the absence of HbA, with HbS moving more slowly towards the cathode.</p> Signup and view all the answers

At what age is Fetal Hemoglobin (HbF) mostly replaced by HbA, and what percentage is replaced?

<p>By age 7 months, 90% of HbF is replaced by HbA.</p> Signup and view all the answers

What role do folic acid antagonists like Methotrexate play in cancer treatment?

<p>They prevent the reduction of Folic Acid to Tetrahydrofolic Acid, blocking nucleic acid synthesis in malignant cells.</p> Signup and view all the answers

Describe the structural components of Cobalamin (Vitamin B12).

<p>Cobalamin consists of a corrin ring and 5,6-dimethylbenzimidazole riboside.</p> Signup and view all the answers

Why is Vitamin B12 not present in vegetable foods?

<p>Neither animals nor plants can synthesize it; it's synthesized by microorganisms in the animal intestine.</p> Signup and view all the answers

What is the function of intrinsic factor in Vitamin B12 absorption?

<p>Intrinsic factor binds to Vitamin B12, facilitating its transport to the ileum for absorption.</p> Signup and view all the answers

What are the potential consequences of Vitamin B12 deficiency?

<p>It can lead to pernicious anemia and neurologic disorders due to myelin sheath damage.</p> Signup and view all the answers

List two food sources of Vitamin K.

<p>Green leafy vegetables like spinach and animal tissues such as liver.</p> Signup and view all the answers

What is the daily requirement of Vitamin K for an average adult?

<p>The requirement is between 70-140 mg/day.</p> Signup and view all the answers

How does Vitamin K function in the body?

<p>It is essential for the conversion of several clotting factors to their active forms.</p> Signup and view all the answers

What role does vitamin K play in the activation of prothrombin?

<p>Vitamin K acts as a cofactor necessary for the carboxylation of glutamic acid to y-carboxy glutamic acid, which is essential for the conversion of prothrombin to active prothrombin.</p> Signup and view all the answers

How does y-carboxy glutamic acid contribute to prothrombin function?

<p>y-Carboxy glutamic acid chelates calcium, enabling the prothrombin-calcium complex to bind to the phospholipid membrane for thrombin conversion.</p> Signup and view all the answers

What are the daily iron requirements for adult females?

<p>Adult females require 18 mg of iron per day.</p> Signup and view all the answers

Describe two factors that enhance iron absorption.

<p>Low pH in the stomach helps liberate iron, and the presence of reducing agents converts ferric iron (Fe³⁺) to ferrous iron (Fe²⁺), which is more easily absorbed.</p> Signup and view all the answers

What is the significance of the heme transporter in iron absorption?

<p>The heme transporter facilitates the direct absorption of heme iron, providing a more efficient source of iron for the body.</p> Signup and view all the answers

What are the consequences of vitamin K deficiency?

<p>Vitamin K deficiency results in a bleeding tendency from minor wounds and is diagnosed by prolonged blood coagulation time.</p> Signup and view all the answers

List two dietary sources of iron.

<p>Organ meats such as liver and plant sources like spinach and whole wheat are good dietary sources of iron.</p> Signup and view all the answers

Name two factors that inhibit iron absorption.

<p>Achlorhydria (absence of hydrochloric acid) and phytates can inhibit iron absorption.</p> Signup and view all the answers

What are the two primary sites of haem biosynthesis and what specific types of haem are produced at each site?

<p>Haem is synthesized in the bone marrow for hemoglobin and in the liver for cytochromes.</p> Signup and view all the answers

Describe the role of ALA Synthase in the synthesis of 5-Amino Levulinic Acid (8-ALA).

<p>ALA Synthase catalyzes the reaction of glycine with succinyl CoA to produce 5-Amino Levulinic Acid.</p> Signup and view all the answers

How many Porphobilinogen molecules are needed to synthesize Uroporphyrinogen?

<p>Four Porphobilinogen molecules are required to synthesize Uroporphyrinogen.</p> Signup and view all the answers

What is the main structural component of folic acid and how is it formed?

<p>Folic acid consists of a pteridine nucleus, P-amino benzoic acid, and glutamic acid, forming pteroic acid plus glutamic acid.</p> Signup and view all the answers

What is the daily requirement of folic acid for adults?

<p>The daily requirement of folic acid for adults is 200 µg.</p> Signup and view all the answers

Identify one major source of one-carbon groups used in one-carbon metabolism.

<p>The beta carbon of serine is the major source of one-carbon groups.</p> Signup and view all the answers

What are two key consequences of folate deficiency?

<p>Folate deficiency leads to macrocytic anemia and gastrointestinal disturbances.</p> Signup and view all the answers

List one function of Tetrahydrofolate (FH4) in metabolism.

<p>Tetrahydrofolate acts as a coenzyme for one-carbon metabolism, facilitating the transfer of one-carbon units.</p> Signup and view all the answers

Study Notes

Biochemistry of Blood

  • The book covers the biochemistry of blood, including blood and carbohydrate metabolism.
  • Different topics within blood biochemistry are detailed.
  • The book appears to be a student resource for biochemistry studies.

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Description

This resource explores the intricate biochemistry of blood, focusing on various aspects such as blood and carbohydrate metabolism. It provides detailed insights into different topics essential for biochemistry students. Perfect for anyone looking to enhance their understanding of blood biochemistry.

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