An aspartic proteinase from human erythrocytes is immunochemically indistinguishable from a non-pepsin, electrophoretically slow moving proteinase from gastric mucosa.
Antiserum raised against an erythrocyte membrane-attached aspartic proteinase precipitates a non-pepsin gastric proteinase. With a monospecific antiserum raised against the non-pepsin gastric proteinase the two enzymes show immunochemical identity. The isoelectric points of both are between 4.5 and 4.6. By SDS-polyacrylamide gel electrophoresis the two proteinases behave the same way. Under non-reducing conditions the main components show molecular weights around 90 000 and after reduction about 58 000. The proteinase may tentatively be classified as cathepsin E.
D016282:Aspartic Acid Endopeptidases; D002402:Cathepsin D / Q000276:immunology; D004586:Electrophoresis; D010450:Endopeptidases / Q000097:blood / Q000276:immunology* / Q000378:metabolism; D004912:Erythrocytes / Q000201:enzymology*; D005753:Gastric Mucosa / Q000201:enzymology*; D006801:Humans; D007526:Isoelectric Point; D008970:Molecular Weight
D010450:Endopeptidases; D016282:Aspartic Acid Endopeptidases; D002402:Cathepsin D