J. Biol. Chem., Vol. 261, Issue 11, 4855-4859, Apr, 1986
Mechanism of the calcium-dependent self-association of bovine prothrombin. Use of a covalent cross-linking reagent to study the reaction
RC Tarvers, CM Noyes, JK Tarvers and RL Lundblad
The present study has made use of a covalent cross-linking agent,
dithiobis(succinimidylpropionate), to study the self-association of
prothrombin and has demonstrated that the covalent dimerization reaction
involves the gamma-carboxyglutamic acid region of prothrombin (1-42 of
582). An essential role for the gamma-carboxyglutamic acid residues of
prothrombin in the association reaction was demonstrated by experiments
that converted gamma-carboxyglutamic acid residues to gamma- methylene
glutamic acid or glutamic acid and resulted in a prothrombin species that
was inactive in our cross-linking assay. Other experiments showed that very
high concentrations of calcium ion inhibit the cross- linkage of
prothrombin. This result is most consistent with an essential
gamma-carboxyglutamic acid-calcium ion-gamma-carboxyglutamic acid bridge(s)
in the calcium-dependent self-associated form of prothrombin.
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