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. 1984 Oct 1;223(1):47–51. doi: 10.1042/bj2230047

Calpain and calpastatin in porcine retina. Identification and action on microtubule-associated proteins.

N Yoshimura, I Tsukahara, T Murachi
PMCID: PMC1144262  PMID: 6093770

Abstract

Two forms of Ca2+-dependent cysteine proteinase (calpain, EC 3.4.22.17) and their specific endogenous inhibitor (calpastatin) were partially purified from porcine retina: calpain I (low-Ca2+-requiring form) was half-maximally activated at 8 microM-Ca2+, and calpain II (high-Ca2+-requiring form) at 250 microM-Ca2+. Both calpain I and calpain II were inhibited by calpastatin. Calpain I from porcine retina was shown to be composed of 83 000- and 29 000-Mr subunits, and calpain II of 80 000- and 29 000-Mr subunits, by the use of monospecific antibodies. Calpains I and II were both found to hydrolyse microtubule-associated proteins 1 and 2 rapidly.

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

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