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What factors lead to conversion of proinsulin to insulin in active form?
We have listed several sites that have all the information you need and have cited the first two sites. From 1 Site Listed: Mosesson1 Harpel and observed that 2-macroglobulin trypsin linked hydrolyzed low molecular weight ester and amide substrates at rates comparable to those of protease free, but the degradation of proteins high molecular weight was strongly inhibited. To reflect this fact, Barrett and Starkey2 introduced the new concept of entrapment steric endopeptidases by 2-macroglobulin. Neurath and Walsh3 have recently examined the role of proteolytic enzymes in the conversion of a variety of enzymes, hormones and other physiologically active proteins from inactive precursors to active forms by limited proteolysis. Many of these proteins are physiologically active in the bloodstream in both precursor and active form. We report here that proinsulin, a large molecular weight polypeptide of 9000, is rapidly hydrolyzed by 2-macroglobulin-bound trypsin. This finding suggests that the protease bound to 2-macroglobulin may be involved in the proteolytic cleavage Limited associated with the activation of precursor molecules and degradation of biologically active polypeptides in the circulation. "From the 2nd Site listed: "A method of simplification, the reproducible production of normal and modified versions of human proinsulin has been developed. A polyhistidine / proinsulin fusion protein was expressed using a prokaryotic expression system and partially purified by affinity chromatography. The disulfide bonds in the polypeptide were formed prior to the removal of the affinity label. The proinsulin cleaved from the fusion protein was then subjected to a final purification step of Semipreparative reversed phase liquid chromatography. Integrity in both normal and mutant proinsulins was confirmed by fingerprinting and mass spectrometry. The different versions of proinsulin will be used to map the residues of the substrate used in the recognition by members of the cleavage site of the Furin / PC family of converting enzymes. "
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