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Characterization of a proteolytically modified form of human prothorombin
- Source :
- Biochemical and biophysical research communications. 94(2)
- Publication Year :
- 1980
-
Abstract
- Treatment of human prothrombin by α chymotrypsin results in the production of a single homogeneous product with an apparent M.W. of 69 000. This product fails to adsorb on barium citrate. NH2-terminal sequence analysis shows that a single cleavage has occurred after tyrosine 44. The proteolytically modified prothrombin which can therefore be referred to as prothrombin (des 1–44), lacks the whole vitamin K dependent part of the molecule. The region of the peptide chain around tyrosine 44 must be particularly exposed to proteolytic attack and serve as a junction between the vitamin K dependent domain and the other structural domains of prothrombin. In the presence of factor Xa alone, prothrombin (des 1–44) is indistinguishable from normal prothrombin when activation is monitored by the appearance of amidolytic activity on S2238. However, activation of prothrombin (des 1–44) is no longer enhanced by the presence of Ca++ and phospholipid in the activation mixture.
- Subjects :
- Vitamin K
Sequence analysis
Biophysics
Phospholipid
Peptide
Cleavage (embryo)
Biochemistry
chemistry.chemical_compound
hemic and lymphatic diseases
Chymotrypsin
Humans
Citrates
Tyrosine
Molecular Biology
Phospholipids
chemistry.chemical_classification
biology
Chemistry
Cell Biology
BARIUM CITRATE
Molecular Weight
Homogeneous
Barium
Factor X
biology.protein
Prothrombin
1-Carboxyglutamic Acid
circulatory and respiratory physiology
Peptide Hydrolases
Subjects
Details
- ISSN :
- 0006291X
- Volume :
- 94
- Issue :
- 2
- Database :
- OpenAIRE
- Journal :
- Biochemical and biophysical research communications
- Accession number :
- edsair.doi.dedup.....cc242300677913e8173a7de55e1515a1