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Isolation and identification of a proteinase from calf thymus that cleaves poly(ADP-ribose) polymerase and histone H1
- 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.
- Subjects :
- Swine
Poly ADP ribose polymerase
Protein subunit
Molecular Sequence Data
Biophysics
Thymus Gland
Biochemistry
Chromatography, Affinity
Chromatography, DEAE-Cellulose
Substrate Specificity
Histones
chemistry.chemical_compound
Histone H1
Structural Biology
Proteinase 3
Animals
Humans
Amino Acid Sequence
Molecular Biology
Peptide sequence
HEPES
chemistry.chemical_classification
Sequence Homology, Amino Acid
biology
Calpain
Caseins
Molecular biology
Rats
Amino acid
Molecular Weight
chemistry
biology.protein
Calcium
Cattle
Rabbits
Poly(ADP-ribose) Polymerases
Subjects
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