Structural differences between rabbit cathepsin E and cathepsin D.
Rabbit cathepsins D and E were isolated from bone marrow. Both enzymes were purified by affinity chromatography on pepstatin-Sepharose 4B and Con A-Sepharose 4B. Purity of the enzymes was ascertained by two-dimensional gel electrophoresis after iodination. The isoelectric point of cathepsin D was found to be 6.95. Cathepsin E was shown to consist of two subunits having molecular masses each of 40 kDa and isoelectric points of 4.60 and 4.65, respectively. The amino-acid composition of cathepsin E was found to be different from that of cathepsin D.
D000596:Amino Acids / Q000032:analysis; D000818:Animals; D001853:Bone Marrow / Q000201:enzymology; D002402:Cathepsin D / Q000032:analysis*; D020059:Cathepsin E; D002403:Cathepsins / Q000032:analysis*; D002846:Chromatography, Affinity; D004591:Electrophoresis, Polyacrylamide Gel; D007525:Isoelectric Focusing; D011817:Rabbits
D000596:Amino Acids; D002403:Cathepsins; D020059:Cathepsin E; D002402:Cathepsin D