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

Authors
Journal
Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology
0167-4838
Publisher
Elsevier
Publication Date
Volume
1338
Issue
1
Identifiers
DOI: 10.1016/s0167-4838(96)00189-6
Keywords
  • Calpain
  • Poly(Adp-Ribose) Polymerase
  • Histone H1
  • (Calf Thymus)
Disciplines
  • Biology

Abstract

Abstract A proteinase was isolated from calf thymus that degraded pADPRT, histone H1 and α-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 α-casein is widely used for the assaying of calpains, more appropriately physiological cellular components (pADPRT and histone H1) specify the thymus proteinase.

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