HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS		QUICK SEARCH:   [advanced] Author: Keyword(s): Year:  Vol:  Page:

This Article Full Text (PDF) Alert me when this article is cited Alert me if a correction is posted Services Email this article to a friend Similar articles in this journal Similar articles in PubMed Alert me to new issues of the journal Download to citation manager Request Permissions Citing Articles Citing Articles via HighWire Citing Articles via Google Scholar Google Scholar Articles by Francis, R. T. Articles by Mann, K. G. Search for Related Content PubMed PubMed Citation Articles by Francis, R. T. Articles by Mann, K. G. Social Bookmarking                      What's this?

J. Biol. Chem., Vol. 261, Issue 21, 9787-9792, 07, 1986

Factor V is a substrate for the transamidase factor XIIIa

RT Francis, J McDonagh and KG Mann

Coagulation Factor V (Mr = 330,000), upon cleavage by thrombin, produces Factor Va, which is composed of two subunits with Mr values of 94,000 and 74,000, along with two activation fragments possessing no known function. Studies were undertaken to assess the ability of the transamidase Factor XIIIa to covalently incorporate the lysine analogs [3H]putrescine and dansylcadaverine into the thrombin-cleaved (activated) and unactivated forms of human and bovine Factor V. The incorporation of either probe into thrombin-activated Factor V proceeded at an initial rate approximately twice that for unactivated Factor V. The extent of the incorporation of [3H]putrescine or dansylcadaverine into activated or unactivated human Factor V was identical; 4 mol of either probe per mol of Factor V. In the case of bovine Factor V, however, while 4 mol of probe were bound per mol of the unactivated pro-cofactor, 5 mol of either lysine analog were covalently linked to 1 mol of thrombin-cleaved Factor V. Polyacrylamide gel fluorography, immunoaffinity chromatography, and immunoprecipitation identified the largest activation fragment of human Factor V (Mr = 150,000) and bovine Factor V (Mr = 120,000) to contain the sites of incorporation of the covalently bound probes. High molecular weight, apparently covalent polymers of Factor V were produced by the action of Factor XIIIa on activated and unactivated human or bovine Factor V. The absence of either probe in the reaction mixtures did not appear to allow an enhancement of protein polymerization.
CiteULike    Complore    Connotea    Del.icio.us    Digg    Reddit    Technorati    What's this?

This article has been cited by other articles:

				S. Yegneswaran, R. M. Mesters, and J. H. Griffin Identification of Distinct Sequences in Human Blood Coagulation Factor Xa and Prothrombin Essential for Substrate and Cofactor Recognition in the Prothrombinase Complex J. Biol. Chem., August 29, 2003; 278(35): 33312 - 33318. [Abstract] [Full Text] [PDF]

				R. A. S. Ariens, T.-S. Lai, J. W. Weisel, C. S. Greenberg, and P. J. Grant Role of factor XIII in fibrin clot formation and effects of genetic polymorphisms Blood, July 18, 2002; 100(3): 743 - 754. [Abstract] [Full Text] [PDF]

				H.P. Kohler and P.J. Grant The role of factor XIIIVal34Leu in cardiovascular disease QJM, February 1, 1999; 92(2): 67 - 72. [Full Text] [PDF]

				Z. Valnickova and J. J. Enghild Human Procarboxypeptidase U, or Thrombin-activable Fibrinolysis Inhibitor, Is a Substrate for Transglutaminases. EVIDENCE FOR TRANSGLUTAMINASE-CATALYZED CROSS-LINKING TO FIBRIN J. Biol. Chem., October 16, 1998; 273(42): 27220 - 27224. [Abstract] [Full Text] [PDF]