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The relationship of structure and function in human Hageman factor. The association of enzymatic and binding activities with separate regions of the molecule

Academic Article
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Overview

authors

  • Revak, S. D.
  • Cochrane, Charles

publication date

  • 1976

journal

  • Journal of Clinical Investigation  Journal

abstract

  • Three regions of the human Hageman factor molecule termed the c, d, and e regions have been defined. Division of the molecule into these three regions is based on the analysis of fragments obtained by enzymatic cleavage during fluid-phase activation. The three regions have the following properties: (a) the c region has a mol wt of 40,000, has the capacity to bind to negatively charged surfaces, and does not have detectable enzymatic activity; (b) the e region possess a mol wt of 28,000 has enzymatic activity, and does not bind to negatively charged surfaces; (c) the d region has a mol wt of 12,000, is located between the c and e fragments but has not been detected as a freely existing polypeptide, and can bind firmly to negatively charged surfaces. The preparation of antibodies specific for the c and e regions is described as well as their use in defining the electrophoretic characteristics of the cde, cd, de, c, and e polypeptide fragments of Hageman factor. Evidence is given showing that the e region, but not the c or d, is released from a negatively charged surface when bound Hageman factor is exposed to proteolytic enzymes or whole plasma and that when this occurs in the presence of normal plasma, the e fragment becomes bound to C1 esterase inhibitor.

subject areas

  • Electrophoresis
  • Factor XII
  • Humans
  • Immunoelectrophoresis
  • Iodine Radioisotopes
  • Kallikreins
  • Kaolin
  • Molecular Weight
  • Prekallikrein
  • Structure-Activity Relationship
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Identity

PubMed Central ID

  • PMC436728

International Standard Serial Number (ISSN)

  • 0021-9738

Digital Object Identifier (DOI)

  • 10.1172/jci108361

PubMed ID

  • 947956
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Additional Document Info

start page

  • 852

end page

  • 860

volume

  • 57

issue

  • 4

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