Literature DB >> 3932093

Characterization of monoclonal antibodies against human protein C specific for the calcium ion-induced conformation or for the activation peptide region.

M Laurell, K Ikeda, S Lindgren, J Stenflo.   

Abstract

Three monoclonal antibodies have been produced that are specific for the activation peptide region in human protein C. These antibodies inhibited the activation of protein C by thrombin and by the thrombin-thrombomodulin complex. A fourth monoclonal antibody specifically recognized the Ca2+-stabilized conformation in protein C. This antibody bound both intact protein C and protein C from which the gamma-carboxyglutamic acid-containing region had been removed by limited proteolysis. These results indicate that this antibody recognizes the conformation in protein C stabilized by Ca2+ bound to the single binding site that is independent of gamma-carboxyglutamic acid.

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Year:  1985        PMID: 3932093     DOI: 10.1016/0014-5793(85)80997-2

Source DB:  PubMed          Journal:  FEBS Lett        ISSN: 0014-5793            Impact factor:   4.124


  3 in total

1.  Isolation and functional characterization of the proenzyme form of the catalytic domains of human C1r.

Authors:  M B Lacroix; C A Aude; G J Arlaud; M G Colomb
Journal:  Biochem J       Date:  1989-02-01       Impact factor: 3.857

2.  Molecular mechanisms of activated protein C resistance. Properties of factor V isolated from an individual with homozygosity for the Arg506 to Gln mutation in the factor V gene.

Authors:  C Aparicio; B Dahlbäck
Journal:  Biochem J       Date:  1996-01-15       Impact factor: 3.857

3.  Characterization of thrombin derived from human recombinant prothrombin.

Authors:  Ann Lövgren; Johanna Deinum; Steffen Rosén; Pia Bryngelhed; Per Rosén; Kenny M Hansson
Journal:  Blood Coagul Fibrinolysis       Date:  2015-07       Impact factor: 1.276

  3 in total

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