title: Biochemical and immunochemical similarity between erythrocyte membrane aspartic proteinase and cathepsin E.
abstract: An aspartic proteinase previously thought to be unique to erythrocyte membranes, termed "EMAP", has been shown to be closely related to cathepsin E. Enzymic comparison revealed that these two enzymes resembled each other in molecular weight, susceptibility to pepstatin and chromatographic behaviors on DEAE-Sephacel and Mono P chromatofocusing columns. They were immunoprecipitated by antiserum against human EMAP in a similar way. Immunochemical similarity between the two enzymes was also substantiated by immunoblot analysis.
authors.affiliation: Department of Pharmacology, Nagasaki University School of Dentistry, Japan.
authors.forename: K
authors.initials: K
authors.lastname: Yamamoto
authors.forename: E
authors.initials: E
authors.lastname: Ueno
authors.forename: H
authors.initials: H
authors.lastname: Uemura
authors.forename: Y
authors.initials: Y
authors.lastname: Kato
mesh_terms: D000936:Antigen-Antibody Complex; D016282:Aspartic Acid Endopeptidases; D020059:Cathepsin E; D002403:Cathepsins / Q000097:blood* / Q000276:immunology; D004591:Electrophoresis, Polyacrylamide Gel; D010450:Endopeptidases / Q000097:blood* / Q000276:immunology / Q000302:isolation & purification; D004910:Erythrocyte Membrane / Q000201:enzymology*; D006801:Humans; D007118:Immunoassay / Q000379:methods; D008970:Molecular Weight
chemical_list: D000936:Antigen-Antibody Complex; D002403:Cathepsins; D010450:Endopeptidases; D016282:Aspartic Acid Endopeptidases; D020059:Cathepsin E