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Structural differences between rabbit cathepsin E and cathepsin D.

C Lapresle·V Puizdar·C Porchon-Bertolotto·E Joukoff·V Turk
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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.

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Amino AcidsAnimalsBone MarrowCathepsin DCathepsin ECathepsinsChromatography, AffinityElectrophoresis, Polyacrylamide GelIsoelectric FocusingRabbitsJournal ArticleResearch Support, Non-U.S. Gov't

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C Lapresle, V Puizdar, C Porchon-Bertolotto, E Joukoff, V Turk. 1986. Structural differences between rabbit cathepsin E and cathepsin D.. https://doi.org/10.1515/bchm3.1986.367.1.523

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