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.