Localization of the metal-induced conformational transition of bovine prothrombin.

Tai, Mindy M.; Furie, Barbara C.; Furie, Bruce

doi:10.1016/s0021-9258(17)43024-9

Cited by 23 publications

(1 citation statement)

References 39 publications

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“…For prothrombin it has been observed that the transition precedes prothrombin-phospholipid interactions (Nelsestuen, 1976). In addition, a number of investigators have isolated antibodies that are specific for the calcium-induced conformer of prothrombin (Madar et al, 1982;Tai et al, 1980Tai et al, , 1984. Others have suggested that the observed quenching might be due to calcium-induced self-association of the protein (Jackson et al, 1979).…”

Section: Discussionmentioning

confidence: 99%

Properties of chemically modified protein S: the effect of the conversion of .gamma.-carboxyglutamic acid to .gamma.-methyleneglutamic acid on functional properties

Walker¹

1986

Biochemistry

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Protein S, the protein cofactor for activated protein C in the proteolytic inactivation of factor Va, was chemically modified with a mixture of morpholine and formaldehyde. This treatment resulted in the conversion of the gamma-carboxyglutamic acid (Gla) residues of this vitamin K dependent protein to gamma-methyleneglutamic acid. With a 10,000-fold molar excess of morpholine and formaldehyde over protein S it was found that between 10 and 11 Gla residues could be modified. The degree of modification was proportional to the concentration of the modifying reagents used. The modification of as few as two residues resulted in the 70% loss of activity. Calcium inhibited the modification of several residues. In the presence of 3.2 mM calcium ion, a derivative with 2.5 residues modified was prepared that appeared to have full activity. Modification of protein S resulted in the alteration of a number of its properties. The quenching of intrinsic fluorescence by calcium decreased. The quenching effect of terbium ions was also decreased. However, the modified protein and the native protein were equivalent when protein-dependent terbium fluorescence was measured. When modified, protein S would no longer bind to phospholipid vesicles. Finally, the ability of protein S to self-associate was decreased by modification. These findings suggest that the gamma-carboxyglutamic acid residues of protein S may play several roles in the maintenance of structure.

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Section: Discussionmentioning

confidence: 99%

Properties of chemically modified protein S: the effect of the conversion of .gamma.-carboxyglutamic acid to .gamma.-methyleneglutamic acid on functional properties

Walker¹

1986

Biochemistry

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Calcium-dependent changes in properties of human prothrombin: A study using high-performance size-exclusion chromatography and gel-permeation chromatography

Tarvers

1985

Archives of Biochemistry and Biophysics

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Anti-human factor IX monoclonal antibodies specific for calcium ion-induced conformations

Sugo

Mizuguchi

Kamikubo

et al. 1990

Thrombosis Research

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Localization of the metal-induced conformational transition of bovine prothrombin.

Cited by 23 publications

References 39 publications

Properties of chemically modified protein S: the effect of the conversion of .gamma.-carboxyglutamic acid to .gamma.-methyleneglutamic acid on functional properties

Properties of chemically modified protein S: the effect of the conversion of .gamma.-carboxyglutamic acid to .gamma.-methyleneglutamic acid on functional properties

Calcium-dependent changes in properties of human prothrombin: A study using high-performance size-exclusion chromatography and gel-permeation chromatography

Anti-human factor IX monoclonal antibodies specific for calcium ion-induced conformations

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