Determination of the Allele Frequencies of Three Polymorphisms in the Promoter Region of the Human Protein C Gene in Three Brazilian Ethnic Groups

1999 ◽  
Vol 49 (1) ◽  
pp. 27-30 ◽  
Author(s):  
Christiane P.O. Mendes ◽  
Christine Hackel ◽  
ValderR. Arruda ◽  
JoyceM. Annichino-Bizzacchi
Keyword(s):  
Ethnic Groups ◽  
Promoter Region ◽  
Protein C ◽  
Allele Frequencies ◽  
Human Protein

scholarly journals Two Mutations in the Promoter Region of the Human Protein C Gene Both Cause Type I Protein C Deficiency by Disruption of Two HNF-3 Binding Sites

1995 ◽  
Vol 270 (41) ◽  
pp. 24216-24221 ◽  
Author(s):  
C. Arnold Spek ◽  
Judith S. Greengard ◽  
John H. Griffin ◽  
Rogier M. Bertina ◽  
Pieter H. Reitsma
Keyword(s):  
Binding Sites ◽  
Promoter Region ◽  
Protein C ◽  
Human Protein ◽  
Type I ◽  
Protein C Deficiency

A Procedure for Isolation of Human Protein C and Protein S as by-Products of the Purification of Factors VII, IX, X and Prothrombin

1983 ◽  
Vol 13 (3) ◽  
pp. 191-214 ◽  
Author(s):  
S. P. Bajaj ◽  
S. I. Rapaport ◽  
S. L. Maki ◽  
S. F. Brown
Keyword(s):  
Protein C ◽  
Protein S ◽  
Human Protein ◽  
By Products

scholarly journals Specificity of activated human protein C

1985 ◽  
Vol 230 (2) ◽  
pp. 497-502 ◽  
Author(s):  
S R Stone ◽  
J Hofsteenge
Keyword(s):  
Amino Acid ◽  
Rate Constant ◽  
Amino Acid Residue ◽  
Protein C ◽  
Activated Protein C ◽  
Order Rate Constant ◽  
Human Protein ◽  
Functional Protein ◽  
Hydrophobic Residues ◽  
Apolar Residue

Peptide p-nitroanilide substrates and peptidylchloromethane inhibitors were used to examine the specificity of activated human Protein C. Substrates with arginine in the P1 position had the highest activity. The best substrates and inhibitors, as judged by the second-order rate constant for their interaction with the enzyme, had an apolar residue in the P2 position. In contrast with thrombin [Kettner & Shaw (1981) Methods Enzymol. 80, 826-842], activated Protein C was able to accommodate large hydrophobic residues such as phenylalanine and leucine in the P2 position. In the P3 position, the enzyme preferred an apolar D-amino acid residue. The results of the present study have also indicated a suitable substrate and inhibitor to be used in the assay of functional protein C and of thrombomodulin.

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