title: B-chain shortening of matrix-bound insulin with pepsin, II. Preparation and properties of camel des-pentapeptide (B26-30)- and des-PheB1-des-pentapeptide (B26-30)- insulin.
abstract: Digestion of matrix-bound camel insulin with pepsin was found to be restricted to the cleavage of the peptide bond between phenylalanine(B25) and tyrosine(B26). Purification of the camel des-pentapeptide(B26-30)-insulin obtained was achieved by gel filtration and ion exchange chromatography, yielding a molecularly uniform product. In the same way, camel des-PheB1-insulin prepared according to a method described for bovine insulin was hydrolyzed with pepsin and purified to give the des-PheB1-despentapeptide(B26-30)-insulin. The biological activity of these modified camel insulins was found to be as much reduced as the corresponding bovine insulin analogues. However, the reduced biological activity of camel des-PheB1-insulin (60%) was a contrast to the fully active bovine des-PheB1-insulin.
mesh_terms: D000596:Amino Acids / Q000032:analysis; D000818:Animals; D001665:Binding Sites; D002162:Camelus / Q000378:metabolism*; D003460:Crystallization; D007328:Insulin / Q000031:analogs & derivatives*; D009842:Oligopeptides / Q000302:isolation & purification; D010434:Pepsin A; D010649:Phenylalanine; D011485:Protein Binding; D014443:Tyrosine
chemical_list: D000596:Amino Acids; D007328:Insulin; D009842:Oligopeptides; D014443:Tyrosine; D010649:Phenylalanine; D010434:Pepsin A