Isolation and some properties of a cathepsin E type proteinase from rat spleen.
Cathepsin E (EC 3.4.23.--) has been isolated from rat spleen. The procedure included autolysis at pH 4.2 which was probably the reason why we isolated a polypeptide of Mr 42 kDa instead of 90 kDa. The latter is reported in the literature to be the Mr of native cathepsin E. The enzyme dissociates under reducing conditions in two identical monomers. In our preparation a mechanism different from reduction must be active producing the 42 kDa polypeptide. This enzyme was hard to distinguish from cathepsin D (EC 3.4.23.5.) which shows similar properties such as size, substrate specificity, stability in 6 M urea, and dependence of the activity on pH. The clear distinction between the two enzymes was proven on the basis of immunochemical reactions. Antibodies to both cathepsins, D and E, did not show any crossreaction with the nonrelated antigen.
Institute of Biochemistry, Faculty of Medicine, Martin-Luther-University Halle/Wittenberg.
B
B
Wiederanders
S
S
Schaper
H
H
Kirschke
D000818:Animals; D015153:Blotting, Western; D002402:Cathepsin D / Q000378:metabolism; D020059:Cathepsin E; D002403:Cathepsins / Q000302:isolation & purification* / Q000378:metabolism; D002852:Chromatography, Ion Exchange; D004591:Electrophoresis, Polyacrylamide Gel; D004795:Enzyme Stability; D007700:Kinetics; D008970:Molecular Weight; D051381:Rats; D013154:Spleen / Q000201:enzymology*; D013379:Substrate Specificity
D002403:Cathepsins; D020059:Cathepsin E; D002402:Cathepsin D