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Investigative Ophthalmology & Visual Science, Vol 27, 1269-1273, Copyright © 1986 by Association for Research in Vision and Ophthalmology

ARTICLES AND REPORTS

The degradation of alpha-crystallin at its carboxyl-terminal portion by calpain in bovine lens

H Yoshida, N Yumoto, I Tsukahara and T Murachi

Bovine lens calpain (Ca2+-dependent cysteine proteinase; EC 3.4.22.17) was shown to catalyze limited proteolysis of A and B chains of alpha- crystallin in vitro. The sites of cleavages were determined by isolating and analyzing the peptide fragments formed using several different methods, including high-performance liquid chromatography, cyanogen bromide cleavage, and carboxypeptidase digestion. The results indicated that calpain cleaved both A and B chains at their respective carboxyl-terminal regions. A chain was cleaved at A(Arg163-Glu164) bond and A(Ser162-Arg163) bond, the former being split with 2.4 times preference over the latter. B chain was cleaved at B(Thr170-Ala171) bond and B (Arg163-Glu164) bond, the former being preferred 6.5 times. Peptide cleavage at any other sites were not detected by the present method of analysis.




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Copyright © 1986 by the Association for Research in Vision and Ophthalmology