ISOLATION AND IDENTIFICATION OF A PROTEINASE FROM CALF THYMUS THAT CLEAVES POLY(ADP-RIBOSE) POLYMERASE AND HISTONE H1

Authors
BUKI KG BAUER PI KUN E
Citation
Kg. Buki et al., ISOLATION AND IDENTIFICATION OF A PROTEINASE FROM CALF THYMUS THAT CLEAVES POLY(ADP-RIBOSE) POLYMERASE AND HISTONE H1, Biochimica et biophysica acta. Protein structure and molecular enzymology, 1338(1), 1997, pp. 100-106
Citations number
37
Categorie Soggetti
Biology,Biophysics
Journal title
Biochimica et biophysica acta. Protein structure and molecular enzymology → ACNP
ISSN journal
01674838
Volume
1338
Issue
1
Year of publication
1997
Pages
100 - 106
Database
ISI
SICI code
0167-4838(1997)1338:1<100:IAIOAP>2.0.ZU;2-P
Abstract
A proteinase was isolated from calf thymus that degraded pADPRT, histo ne H1 and alpha-casein in a Ca2+-dependent manner. In a five-step proc edure, a homogenous proteinase was obtained with a subunit structure o f 80 and 30 kDa. The amino-acid homology of an internal sequence as we ll as kinetic and inhibitor assays identified the proteinase as calpai n I. It is suggested that even though the general substrate alpha-case in is widely used for the assaying of calpains, more appropriately phy siological cellular components (pADPRT and histone H1) specify the thy mus proteinase.