Preparation of Insulin
Preparation of insulin involves extraction or recombinant DNA technology to produce purified hormone for diabetes treatment.
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Formation of Preproinsulin:
- Insulin synthesis begins with preproinsulin (110 amino acids), synthesized in the rough endoplasmic reticulum.
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Conversion to Proinsulin:
- Preproinsulin is processed in the Golgi apparatus to form proinsulin, an inactive precursor.
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Folding and Bond Formation:
- Proinsulin folds to form three disulfide bonds, linking the A-chain and B-chain.
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Packaging into Vesicles:
- Folded proinsulin is packaged into secretory vesicles for further processing.
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Cleavage by Enzymes:
- Enzymes (Proprotein Convertase 1/3 and Proprotein Convertase 2) cleave the C-peptide from proinsulin.
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Final Processing:
- Carboxypeptidase E removes terminal amino acids, yielding active insulin.
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Active Insulin:
- Active insulin consists of:
- Chain A: 21 amino acids.
- Chain B: 30 amino acids.
- Chains are connected by two disulfide bonds.
- Active insulin consists of:
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Secretion:
- Active insulin is secreted into the bloodstream to regulate blood sugar and metabolic processes.
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