Evidence for an Ester Bond between Thrombin and Heparin Cofactor

Autor:	Whyte G. Owen, Barbara L Poole, Elizabeth Yoder, George D Penick
Rok vydání:	1976
Předmět:	Guanidinium chloride Hematology Medicinal chemistry Dissociation (chemistry) Gel permeation chromatography chemistry.chemical_compound Hydroxylamine Thrombin chemistry Affinity chromatography Sodium hydroxide Covalent bond medicine medicine.drug
Zdroj:	Thrombosis and Haemostasis. 35:087-095
ISSN:	2567-689X 0340-6245
DOI:	10.1055/s-0038-1647914
Popis:	SummaryHeparin cofactor, a thrombin inhibitor, is purified from human plasma by affinity chromatography on heparin-agarose. The nature of the binding between thrombin and the inhibitor is studied by treatment of the complex with 6 M guanidinium chloride, hydroxylamine, and dilute alkali. The complex is not dissociated during gel chromatography in 6 M guanidinium chloride. This result supports an earlier proposal that formation of the complex includes the formation of a covalent bond. Treatment of dodecyl sulfate-denatured complex with hydroxylamine results in dissociation of the complex to yield free thrombin and heparin cofactor. Hydroxylamine does not dissociate the complex unless it is denatured. The complex is also dissociated in dilute sodium hydroxide (pH 12) solutions. These results indicate that the covalent bond between thrombin and the inhibitor is a carboxylic ester.
Databáze:	OpenAIRE
Externí odkaz:	https://explore.openaire.eu/search/publication?articleId=doi_________::49acbc835d9c37aa61aac1f8466b6b19 https://doi.org/10.1055/s-0038-1647914 Zobrazit plný text záznamu