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Questions and Answers
What is the primary function of hemoglobin in the body?
What is the primary function of hemoglobin in the body?
Which structural characteristic differentiates hemoglobin from myoglobin?
Which structural characteristic differentiates hemoglobin from myoglobin?
In which condition is hemoglobinuria likely to occur?
In which condition is hemoglobinuria likely to occur?
What distinguishes myoglobin from hemoglobin in terms of oxygen binding?
What distinguishes myoglobin from hemoglobin in terms of oxygen binding?
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What color does urine typically become in hemoglobinuria?
What color does urine typically become in hemoglobinuria?
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What test can differentiate between hemoglobinuria and myoglobinuria?
What test can differentiate between hemoglobinuria and myoglobinuria?
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What type of oligomeric structure does hemoglobin have?
What type of oligomeric structure does hemoglobin have?
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Which of the following is NOT a known cause of hemoglobinuria?
Which of the following is NOT a known cause of hemoglobinuria?
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Which statement about myoglobin's structure is correct?
Which statement about myoglobin's structure is correct?
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What is the main role of the heme group in hemoglobin?
What is the main role of the heme group in hemoglobin?
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Study Notes
Biochemistry 1 (PHB231) - Hemoglobin Precipitation
- Course: Biochemistry 1 (PHB231)
- Department: Biochemistry Department, Faculty of Pharmacy
- University: October University
- Prepared by: A.L. Heba Elrefaie and T.A. Mariam Sabry
Heme Proteins
- Hemeproteins are proteins containing a heme prosthetic group.
- Functions include oxygen transport, oxygen reduction, and electron transfer.
Hemoglobin and Myoglobin
- Most abundant heme proteins in humans.
- Heme group's primary function is reversible binding of molecular oxygen.
Hemoglobin (Function)
- Present in red blood cells (RBCs).
- Main function: transporting oxygen from lungs to tissues.
- Also transports carbon dioxide from tissues to lungs.
Myoglobin (Function)
- Located in the heart and skeletal muscles.
- Carries and stores oxygen in muscle cells.
Hemoglobin (Structure)
- Quaternary structure.
- Composed of four subunits (2 alpha chains and 2 beta chains).
- Each chain contains a heme group; thus, hemoglobin can bind to four oxygen molecules.
Myoglobin (Structure)
- Tertiary structure.
- Composed of one polypeptide chain (8 alpha helices designated A-H).
- Contains one heme group, binding to only one oxygen molecule.
Hemoglobinuria (Abnormalities)
- Presence of hemoglobin in urine, causing a dark red or brown color.
- Causes:
- Intravascular hemolysis (RBC lysis in the urinary tract).
- Extravascular hemolysis (RBC lysis at a specific gravity less than 1.010).
Hemoglobin and Myoglobin (Abnormalities)
- Excess hemoglobin:
- Hemoglobin exceeds the amount of the hemoglobin-haptoglobin complex.
- Hemolytic anemia.
- Severe burns.
- Blood transfusion reactions.
- Strenuous exercise.
- Infections
Myoglobinuria (Abnormalities)
- Presence of myoglobin in urine, causing a dark red or brown color.
- Causes:
- Rhabdomyolysis.
- This is muscle tissue breakdown and subsequent release of intracellular contents into the bloodstream, including myoglobin.
- Distal tubular toxicity
Ammonium Sulphate Precipitation Test (Chemical Tests)
- Used to distinguish between hemoglobinuria and myoglobinuria.
- Based on the saturation level of ammonium sulfate:
- Hemoglobin precipitates at 80% saturation.
- Myoglobin precipitates at 100% saturation.
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Description
This quiz covers important aspects of hemoglobin and myoglobin, focusing on their structures, functions, and roles in oxygen transport and storage. It is designed for students enrolled in the Biochemistry 1 (PHB231) course at October University. Dive into the world of heme proteins and understand their significance in human physiology.
