Literature DB >> 7400308

Electron microsocpy of plasmic fragments of human fibrinogen as related to trinodular structure of the intact molecule.

W E Fowler, L J Fretto, H P Erickson, P A McKee.   

Abstract

We have examined rotary shadowed, purified plasmic fragments of human fibrinogen with the electron microscope and have determined the relation of these fragments to the intact fibrinogen molecule. Both intact fibrinogen and its earliest cleavage product, fragment X, are trinodular. The next largest product, fragment Y, consists of two linked nodules. The two terminal products, fragments D and E, are single nodules. From measurements of simultaneously shadowed specimens of these different species, we conclude that the outer nodules of the trinodular fibrinogen molecule are the fragment D-containing regions and the central nodule is the fragment E-containing region.

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Year:  1980        PMID: 7400308      PMCID: PMC371504          DOI: 10.1172/JCI109834

Source DB:  PubMed          Journal:  J Clin Invest        ISSN: 0021-9738            Impact factor:   14.808


  21 in total

Review 1.  Structural aspects of the fibrinogen to fibrin conversion.

Authors:  R F Doolittle
Journal:  Adv Protein Chem       Date:  1973

2.  High molecular weight derivatives of human fibrinogen produced by plasmin. II. Mechanism of their anticoagulant activity.

Authors:  V J Marder; N R Shulman
Journal:  J Biol Chem       Date:  1969-04-25       Impact factor: 5.157

3.  High molecular weight derivatives of human fibrinogen produced by plasmin. I. Physicochemical and immunological characterization.

Authors:  V J Marder; N R Shulman; W R Carroll
Journal:  J Biol Chem       Date:  1969-04-25       Impact factor: 5.157

4.  [Electron microscopy study on the various stages of fibrin formation].

Authors:  L Pouit; G Marcille; M Suscillon; D Hollard
Journal:  Thromb Diath Haemorrh       Date:  1972-07-31

5.  Difference in conformation of fibrinogen degradation products as revealed by hydrogen exchange and spectropolarimetry.

Authors:  A Z Budzynski
Journal:  Biochim Biophys Acta       Date:  1971-03-23

6.  A facile separation of fragments D and E from the fibrinogen-fibrin degradation products of three mammalian species.

Authors:  J P Chen; H M Shurley; M Vickroy
Journal:  Biochem Biophys Res Commun       Date:  1974-11-06       Impact factor: 3.575

7.  Formation of highly ordered polymers from fibrinogen and fibrin degradation products.

Authors:  S Niewiarowski; G J Stewart; V J Marder
Journal:  Biochim Biophys Acta       Date:  1970-11-17

8.  Conformation of fibrinogen: calorimetric evidence for a three-nodular structure.

Authors:  J W Donovan; E Mihalyi
Journal:  Proc Natl Acad Sci U S A       Date:  1974-10       Impact factor: 11.205

9.  The reliability of molecular weight determinations by dodecyl sulfate-polyacrylamide gel electrophoresis.

Authors:  K Weber; M Osborn
Journal:  J Biol Chem       Date:  1969-08-25       Impact factor: 5.157

10.  [Electron microscopical studies on the form and macromolecular construction of fibrinogen molecules and fibrin fibers].

Authors:  G Köppel
Journal:  Z Zellforsch Mikrosk Anat       Date:  1967
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  3 in total

1.  Structure of the fibrin protofibril.

Authors:  W E Fowler; R R Hantgan; J Hermans; H P Erickson
Journal:  Proc Natl Acad Sci U S A       Date:  1981-08       Impact factor: 11.205

2.  Substructure of human von Willebrand factor.

Authors:  W E Fowler; L J Fretto; K K Hamilton; H P Erickson; P A McKee
Journal:  J Clin Invest       Date:  1985-10       Impact factor: 14.808

3.  Electron microscopy of human factor VIII/Von Willebrand glycoprotein: effect of reducing reagents on structure and function.

Authors:  K Ohmori; L J Fretto; R L Harrison; M E Switzer; H P Erickson; P A McKee
Journal:  J Cell Biol       Date:  1982-11       Impact factor: 10.539

  3 in total

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