Occurrence of cathepsin D isozymes with different specificities in monkey skeletal muscle.
Cathepsin D was highly purified from the skeletal muscle of Japanese monkey (Macaca fuscata fuscata) by a procedure including affinity chromatography on concanavalin A-Sepharose and pepstatin-Sepharose, and then resolved into ten isozymes (A through J) by isoelectric focusing. When examined for specificity toward oxidized insulin B chain, isozyme A was highly specific and cleaved exclusively the Leu15-Tyr16 bond, whereas isozyme F was less specific, cleaving the Leu15-Tyr16 and Glu13-Ala14 bonds, with slower cleavages at several other bonds. These results demonstrate for the first time the occurrence of isozymes with different specificities among cathepsin D isozymes obtained from a single source.
Tanji
M
M
Department of Biophysics and Biochemistry, Faculty of Science, University of Tokyo, Japan.
Kageyama
T
T
Takahashi
K
K
D000595:Amino Acid Sequence; D000818:Animals; D002402:Cathepsin D / Q000378:metabolism*; D002454:Cell Differentiation; D002846:Chromatography, Affinity; D007525:Isoelectric Focusing; D007527:Isoenzymes / Q000378:metabolism; D008251:Macaca; D008969:Molecular Sequence Data; D024510:Muscle Development; D009132:Muscles / Q000201:enzymology*; D013379:Substrate Specificity
D007527:Isoenzymes; D002402:Cathepsin D