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Internalization of the amino terminal 1-78 sequence of the gamma-chain of native fibrinogen and exposure associated with catabolism and plasmin cleavage

Academic Article
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Overview

authors

  • Cierniewski, C. S.
  • Edgington, Thomas

publication date

  • 1979

journal

  • Biochimica et Biophysica Acta  Journal

abstract

  • Specific antibodies of the gamma 1--78 peptide of human fibrinogen were employed in binding assays and in equilibrium competitive inhibition assays to analyze the expression of gamma 1--78 antigenic determinants as an indication of the relative exposure of the gamma 1--78 sequence in the E domain of fibrinogen, high solubility fibrinogen subfractions I-8 and I-9, and plasmic cleavage fragments of fibrinogen and fibrin. A very limited exposure of gamma 1--78 sequences was found to occur concomitant with proteolytic deletions of the major carboxyterminal segment of the A alpha chains in fgI-8, fgI-9. Exposure of gamma 1--78 is not influenced by further proteolysis to fg-X which is associated with B beta 1--43 deletion. Further proteolysis to fg-Y, which is associated with deletion of beta 43--53 and of one of the D domains, is associated with additional exposure of gamma 1--78. This is not significantly influenced by further proteolysis to fg-E with deletion of the second D domain, deletion of A alpha 1--19, and proteolysis at the carboxyterminal aspects of the E domain chains.

subject areas

  • Amino Acid Sequence
  • Antibodies
  • Epitopes
  • Fibrinogen
  • Fibrinolysin
  • Humans
  • Peptide Fragments
  • Protein Binding
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Identity

International Standard Serial Number (ISSN)

  • 0006-3002

Digital Object Identifier (DOI)

  • 10.1016/0005-2795(79)90195-8

PubMed ID

  • 94836
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Additional Document Info

start page

  • 32

end page

  • 43

volume

  • 580

issue

  • 1

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