The digestion of the oxidized B chain of insulin by human neutrophile proteases: elastase and chymotrypsin-like protease.
The specificities of human neutrophile elastase and chymotrypsin-like protease towards oxidized insulin B chain were studied. The neutrophile elastase was found to differ from porcine pancreatic elastase in its specificity towards insulin B chain. The neutrophile elastase preferred mostly valine near the cleaved bond in contrast to pancreatic elastase which preferred alanine as well as valine near the cleaved bond. Human neutrophile chymotrypsin-like protease was found to cleave mostly bonds involving leucine and phenylalanine.
D000409:Alanine; D000818:Animals; D002918:Chymotrypsin / Q000097:blood*; D006801:Humans; D007328:Insulin; D007930:Leucine; D009504:Neutrophils / Q000201:enzymology*; D010196:Pancreatic Elastase / Q000097:blood*; D010447:Peptide Hydrolases / Q000097:blood*; D010649:Phenylalanine; D013045:Species Specificity; D013379:Substrate Specificity; D013552:Swine; D014633:Valine
D007328:Insulin; D010649:Phenylalanine; D010447:Peptide Hydrolases; D002918:Chymotrypsin; D010196:Pancreatic Elastase; D007930:Leucine; D014633:Valine; D000409:Alanine