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PubMed · 953054

Pig prothrombin: purification and properties.

F A Leone·G Chiericayo·J C Say·J R Giglio
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Abstract

A procedure for the preparation of highly purified pig prothrombin is described. Compared to the initial clotting activity of the starting plasma, this protein was purified 776 times with a final yield of 8 per cent. The purified zymogen showed a specific activity of 1,460 NH units/mg of protein , a molecular weight of 65,000 as determined by SDS-polyacrylamide disc gel electroesis, E 1.0 mg/ml 1.0 cm, 280 nm = 1.45 at pH 7.0 and the following amino acid composition: Asx 51, Thr 38, Glx 62, Pro 23, Gly44, Ala 25, Half-Cys 30, Val 35, Met 3, Ile 30, Leu 32, Tyr 19, Phe 22, Lys 36, His 8, Arg 28, and Trp 13, which accounts for a minimum molecular weight of 59,370 (carbohydrates not computed). Alanine was found as the only N-terminal residue. Carboxypeptidases A and B failed to release any C-terminal residue. By hydrazinolysis however 0.4 mole of serine was released per mole of prothrombin. The activation of crude and chromatographed pig prothrombin was investigated.

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Amino AcidsAnimalsElectrophoresis, DiscHumansMolecular WeightProthrombinSpecies SpecificitySwineJournal Article

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BibTeXRIS

F A Leone, G Chiericayo, J C Say, J R Giglio. 1976. Pig prothrombin: purification and properties.. https://doi.org/10.1016/s0300-9084(76)80219-2

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