Oct 21, 1986

Possible basis for the apparent surface selectivity of the contact activation of human blood coagulation factor XII

Biochemistry
M A GriepG L Nelsestuen

Abstract

The activation of factor XII by the proteases factor XIIa and kallikrein is known to be greatly enhanced by certain negatively charged surfaces. Studies that compared factor XII surface binding to factor XII activation found that binding alone was insufficient to account for surface enhancement of the activation rate. The temperature dependence of the reaction showed unusual behavior that may be related to the conformational change of factor XII following binding; the rate of factor XII activation had a relatively low temperature optimum (0-47 degrees C) that was sensitive to choice of surface and salt concentration. In temperature studies, below 47 degrees C, the decrease in the activation rate was not related to the thermal denaturation of enzyme or substrate, nor to the choice of activator enzyme (factor XIIa or kallikrein), nor to the species of factor XII (human or bovine) but to a behavior, designated a thermal transition, associated with the surface or the protein-surface interaction. The previously reported surface selectivity of contact activation is possible due to the temperature characteristics and other properties of the thermal transition; a surface that has a low-temperature thermal transition and that is highly ...Continue Reading

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Mentioned in this Paper

Thermodynamics
Peptide Fragments
Sodium Chloride, (24)NaCl
Hageman-Factor Fragments
Factor XII
Enzyme Activation
Osmolality
KLK1
Scattering, Radiation
Padutin

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