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Isolation and identification of a proteinase from calf thymus that cleaves poly(ADP-ribose) polymerase and histone H1

Authors :
Kalman G. Buki
Ernest Kun
Pal I. Bauer
Source :
Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology. 1338:100-106
Publication Year :
1997
Publisher :
Elsevier BV, 1997.

Abstract

A proteinase was isolated from calf thymus that degraded pADPRT, histone H1 and alpha-casein in a Ca(2+)-dependent manner. In a five-step procedure, a homogenous proteinase was obtained with a subunit structure of 80 and 30 kDa. The amino-acid homology of an internal sequence as well as kinetic and inhibitor assays identified the proteinase as calpain I. It is suggested that even though the general substrate alpha-casein is widely used for the assaying of calpains, more appropriately physiological cellular components (pADPRT and histone H1) specify the thymus proteinase.

Details

ISSN :
01674838
Volume :
1338
Database :
OpenAIRE
Journal :
Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology
Accession number :
edsair.doi.dedup.....dce638041dc4211348f396a763c31f51
Full Text :
https://doi.org/10.1016/s0167-4838(96)00189-6