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. 1979 Dec 1;183(3):513–517. doi: 10.1042/bj1830513

The nature of the slow metal ion-dependent conformational transition in bovine prothrombin.

H C Marsh, M E Scott, R G Hiskey, K A Koehler
PMCID: PMC1161631  PMID: 540028

Abstract

Kinetic parameters characterizing the slow structural isomerization observed via metal ion-dependent intrinsic fluorescence quenching of bovine prothrombin Fragment 1 have been determined. From forward and reverse rate constants, an equilibrium constant of approx. 0.25 is calculated. This result is consistent with the hypothesis that there exists, in the absence of metal ions, an equilibrium between two forms of bovine Fragment 1, one of which can interact rapidly with Ca2+ and subsequently with phospholipid. The other form of Fragment 1 cannot interact with Ca2+ in a manner that yields a phospholipid-binding form of the protein. Interconversion of these two forms of Fragment 1 occurs and may involve the isomerization of a proline residue.

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

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