| 1. | Preproinsulin is a proinsulin molecule with a signal peptide attached to its N-terminus.
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| 2. | In the RER the proinsulin folds into the correct conformation and 3 disulfide bonds are formed.
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| 3. | -- Proinsulin is a precursor of insulin, which the body makes to convert sugar to energy.
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| 4. | The signal peptide is cleaved as the polypeptide is translocated into lumen of the RER, forming proinsulin.
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| 5. | When insulin was originally purified from bovine or porcine pancreata, all the proinsulin was not fully removed.
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| 6. | This can be described as an iatrogenic injury due to slight differences between the proinsulin of different species.
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| 7. | Proinsulin C-peptide was first described in 1967 in connection with the discovery of the insulin biosynthesis pathway.
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| 8. | The signal sequence is cleaved from the N-terminus of the peptide by a signal peptidase, leaving proinsulin.
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| 9. | Insulin resistance in Type 2 diabetes produces a greater demand for insulin production which results in the secretion of proinsulin.
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| 10. | More modification can occur in the secretory vesicles ( for example insulin is cleaved from proinsulin in the secretory vesicles ).
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