Location of peptide fragments in the fibrinogen molecule by immunoelectron microscopy

J. N. Telford, J. A. Nagy, Paul Hatcher, H. A. Scheraga

Research output: Contribution to journalArticle

32 Citations (Scopus)

Abstract

Antibodies to the disulfide knot fragment of bovine fibrinogen have been used to locate the site of this fragment within the intact fibrinogen molecule. The antibodies were isolated from rabbit antifibrinogen antisera by affinity chromatography. Electron micrographs of reaction mixtures of bovine fibrinogen and antibodies against the disulfide knot fragment showed pairs of fibrinogen molecules crosslinked by antibody molecules as well as higher order antibody-fibrinogen complexes. From an electron microscopic investigation of the crosslinked material, we conclude that the disulfide knot lies within the central nodule of the trinodular fibrinogen molecule. Antibodies to fragment H were used in the same manner to locate this fragment within the outer nodules of the human fibrinogen molecule.

Original languageEnglish (US)
Pages (from-to)2372-2376
Number of pages5
JournalProceedings of the National Academy of Sciences of the United States of America
Volume77
Issue number5 II
StatePublished - Dec 1 1980
Externally publishedYes

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Peptide Fragments
Immunoelectron Microscopy
Fibrinogen
Antibodies
Disulfides
Electrons
Immunoglobulin Fragments
Affinity Chromatography
Immune Sera
Rabbits

All Science Journal Classification (ASJC) codes

  • General

Cite this

Location of peptide fragments in the fibrinogen molecule by immunoelectron microscopy. / Telford, J. N.; Nagy, J. A.; Hatcher, Paul; Scheraga, H. A.

In: Proceedings of the National Academy of Sciences of the United States of America, Vol. 77, No. 5 II, 01.12.1980, p. 2372-2376.

Research output: Contribution to journalArticle

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AU - Hatcher, Paul

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AB - Antibodies to the disulfide knot fragment of bovine fibrinogen have been used to locate the site of this fragment within the intact fibrinogen molecule. The antibodies were isolated from rabbit antifibrinogen antisera by affinity chromatography. Electron micrographs of reaction mixtures of bovine fibrinogen and antibodies against the disulfide knot fragment showed pairs of fibrinogen molecules crosslinked by antibody molecules as well as higher order antibody-fibrinogen complexes. From an electron microscopic investigation of the crosslinked material, we conclude that the disulfide knot lies within the central nodule of the trinodular fibrinogen molecule. Antibodies to fragment H were used in the same manner to locate this fragment within the outer nodules of the human fibrinogen molecule.

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