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. 1977;36(11-12):1531-5.

Studies on bovine spleen cathepsin D

V Turk, I Kregar, F Gubensek, S Lapanje, I Urh, M Kovacic
  • PMID: 616700

Studies on bovine spleen cathepsin D

V Turk et al. Acta Biol Med Ger. 1977.

Abstract

The purification procedure of cathepsin D which includes autolysis results in the destruction of the molecule to smaller polypeptide chains. Pure catepsin D obtained by the method which includes affinity chromatography, contains single polypeptide chain of 42000 daltons. The N-terminal amino acid is glycine. The specificity was studied using synthetic substrates. CD measurement of cathepsin D shows mainly unordered structure, about 26% of beta-structure and only 5% of alpha-helix. Binding of pepstatin shows pronounced changes in the CD spectrum between 250 and 300 nm; above 7.5 no interaction was observed.

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