| Literature DB >> 3741628 |
C Lapresle, V Puizdar, C Porchon-Bertolotto, E Joukoff, V Turk.
Abstract
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.Entities:
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Year: 1986 PMID： 3741628 DOI： 10.1515/bchm3.1986.367.1.523
Source DB: PubMed Journal: Biol Chem Hoppe Seyler ISSN： 0177-3593