The specificity of purified porcine pancreatic elastase.
An electrophoretically homogeneous elastase preparation free from tryptic and chymotryptic activities was obtained by chromatography on DEAE-Sephadex and CM-cellulose. This preparation exhibits a narrower specificity towards peptide bonds than that observed by Naughton & Sanger (1961). With oxidized insulin B chain as substrate, the fastest breaks occur between alanine-14 and leucine-15 and between valine-18 and cysteic acid-19. The bond between glycine-23 and phenylalanine-24 is also efficiently hydrolysed. Other bonds hydrolysed are that between valine-12 and glutamic acid-13 and that between serine-9 and histidine-10. Oxidized insulin A chain is hydrolysed only at one of two points, between alanine-8 and serine-9 or between serine-12 and leucine-13, and the rate of hydrolysis is very low.
D000409:Alanine; D000818:Animals; D002845:Chromatography; D003545:Cysteine; D004586:Electrophoresis; D005971:Glutamates; D005998:Glycine; D006639:Histidine; D007328:Insulin; D007930:Leucine; D010179:Pancreas / Q000032:analysis*; D010196:Pancreatic Elastase / Q000302:isolation & purification*; D010649:Phenylalanine; D012694:Serine; D013552:Swine; D014633:Valine
D005971:Glutamates; D007328:Insulin; D012694:Serine; D010649:Phenylalanine; D006639:Histidine; D010196:Pancreatic Elastase; D007930:Leucine; D014633:Valine; D003545:Cysteine; D000409:Alanine; D005998:Glycine