Peptide maps of five human pepsin isoenzymes and other aspartic proteinases.
Peptide maps of five individual human pepsins were developed using reversed-phase high-performance liquid chromatography after protein digestion with either Staphylococcus aureus proteinase (V8) or alpha-chymotrypsin. Human pepsins 3a, 3b and 3c produced almost identical peptide maps suggestive of proteins with very similar amino acid sequences. The map for human pepsin 1 was similar to pepsin 3b (the most predominant human pepsin) but less than half the expected amount of each equivalent peptide fragment was generated, indicating that the actual mass of digested protein used was less than the dry weight measurement would suggest, probably as a result of carbohydrate attached to pepsin 1. Comparison of human pepsin 3b maps with other aspartic proteinases confirmed a significant homology with swine pepsin A but not with endothiapepsin. The alpha-chymotrypsin digests compared with V8 gave more complex peptide maps as a result of its broader bond cleavage specificities.
Jones
A T
AT
Department of Clinical Chemistry, Royal Liverpool University Hospital, UK.
Roberts
N B
NB
D000818:Animals; D016282:Aspartic Acid Endopeptidases / Q000737:chemistry*; D002851:Chromatography, High Pressure Liquid; D002918:Chymotrypsin; D006801:Humans; D007527:Isoenzymes / Q000737:chemistry*; D010434:Pepsin A / Q000737:chemistry*; D010449:Peptide Mapping; D012697:Serine Endopeptidases; D013056:Spectrophotometry, Ultraviolet; D013552:Swine
D007527:Isoenzymes; D012697:Serine Endopeptidases; D002918:Chymotrypsin; C028344:glutamyl endopeptidase; D016282:Aspartic Acid Endopeptidases; C042466:Endothia aspartic proteinase; D010434:Pepsin A