Structure-function relationships in heparin cofactor II: chemical modification of arginine and tryptophan and demonstration of a two-domain structure

Archives of Biochemistry and Biophysics
F C ChurchM J Griffith

Abstract

Heparin cofactor II and antithrombin III are plasma proteins functionally similar in their ability to inhibit thrombin at accelerated rates in the presence of heparin. To further characterize the structural and functional properties of human heparin cofactor II as compared to antithrombin III, we studied the possible significance of arginyl and tryptophanyl residues and the changes in protein structure and activity during guanidinium chloride (GdmCl) denaturation. Both antithrombin and heparin cofactor activities of heparin cofactor II are inactivated by the arginine-specific reagent, 2,3-butanedione. Saturation kinetics are observed during modification and suggest formation of a reversible protease inhibitor-butanedione complex. Quantitation of arginyl residues following butanedione modification shows a loss of about four residues for total inactivation, one of which is essential for antithrombin activity. Arginine-modified heparin cofactor II did not bind to heparin-agarose and implies a role for the other modified arginyl residues during heparin cofactor activity. N-Bromosuccinimide oxidation (20 mol of reagent/mol of protein) of heparin cofactor II results in modification of approximately two tryptophanyl residues with no c...Continue Reading

References

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Citations

Jan 1, 1989·Annals of the New York Academy of Sciences·C W PrattF C Church
Oct 14, 1987·Biochemical and Biophysical Research Communications·F C ChurchH C Whinna
Jan 1, 1995·International Journal of Peptide and Protein Research·L G MeltonB W Erickson
Aug 15, 1986·Analytical Biochemistry·F C Church, H C Whinna

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