[CITATION][C] Proteolytic formation and properties of gamma-carboxyglutamic acid-domainless protein C.

NL Esmon, LE DeBault, CT Esmon - Journal of Biological Chemistry, 1983 - Elsevier
NL Esmon, LE DeBault, CT Esmon
Journal of Biological Chemistry, 1983Elsevier
Methods Assay of Protein C Activation-Initial rates of protein c activation with purified
thrombomodulin and thrombin were determined by stopping the activation reaction and
measuring activated protein C formed in the reaction mixture at selected time points. All
activations were performed in 0.1 M NaCl, 0.02 M Tris-HC1, lO mg/ml of bovine serum
albumin, pH 7.5, at 37" C. Gelatin (0.18) replaced the bovine serum albumin in those cases
where the effect of calcium was being determined. In these experiments, aU proteins were …
Methods Assay of Protein C Activation-Initial rates of protein c activation with purified thrombomodulin and thrombin were determined by stopping the activation reaction and measuring activated protein C formed in the reaction mixture at selected time points. All activations were performed in 0.1 M NaCl, 0.02 M Tris-HC1, lO mg/ml of bovine serum albumin, pH 7.5, at 37" C. Gelatin (0.18) replaced the bovine serum albumin in those cases where the effect of calcium was being determined. In these experiments, aU proteins were dialyzed against Chelex-treated buffer (Bio-Rad) before use and the buffer was also
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