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Thromb Haemost 1962; 08(01): 021-036
DOI: 10.1055/s-0038-1655409
Originalarbeiten — Original Articles — Travaux Originaux
Schattauer GmbH

Immunochemical Studies on Proteins Important in Blood Coagulation[*]

Marion I. Barnhart
1   Department of Physiology and Pharmacology Wayne State University College of Medicine, Detroit, Michigan, USA
,
G. F Erson
1   Department of Physiology and Pharmacology Wayne State University College of Medicine, Detroit, Michigan, USA
,
W. J Baker   **
1   Department of Physiology and Pharmacology Wayne State University College of Medicine, Detroit, Michigan, USA
› Author Affiliations
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Publication History

Publication Date:
14 May 2019 (online)

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Summary

This report draws attention to the fact that only minute quantities of purified serum proteins (1 —15 μg/kg body weight) are required to stimulate antibody production. Injection of amounts greater than 1 mg/kg either is a waste or favors the production of non-specific antisera. Potent antisera can be produced in rabbits with a single intramuscular injection using either Al(OH)3 gel or Amphojel as an adjuvant.

A number of purified plasma protein preparations which appear homogenous by ultra centrifugation or biological activity studies actually contain several antigenic components and are immunologically heterogeneous, when checked with highly specific antisera.

Fibrinogen prepared by alcohol fractionation and tannic acid purification was found to be free of prothrombin, antihemophilic factor and Profibrinolysin. Both Immunoelectrophoresis and double diffusion in agar indicated a homogeneous preparation.

Fibrinogens prepared from human, canine and bovine plasmas exhibited a low species specificity.

* Aided by a research grant from the Michigan Heart Association and research grant H-4712 from the National Heart Institute, National Institutes of Health, United States Public Health Service.


** Present address Ortho Research Foundation, Raritan, N. J.


 

  • References

  • 1 Freund J. Some aspects of active immunization.. Ann. Rev. Microbiol. 1947; 1: 291
    CrossrefPubMedGoogle Scholar
  • 2 Cohn M. Production of antibodies in experimental animals.. Meth. med. Res. 1952; 5: 271
    PubMedGoogle Scholar
  • 3 Ware A. G, Guest M. M, Seegers W. H. Fibrinogen: With special reference to its preparation and certain properties of the product.. Arch. Biochem. 1947; 13: 231
    PubMedGoogle Scholar
  • 4 Blombäck B. Studies on fibrinogen: Its purification and conversion into fibrin.. Acta physiol. scand. 1958; 43: 1
    CrossrefPubMedGoogle Scholar
  • 5 Simonetti C, Casillas G, Pavlovsky A. Purification du facteur VIII antihémophilique (FAH).. Hémostase 1961; 1: 57
    PubMedGoogle Scholar
  • 6 Anderson G. F. Prothrombin synthesis in the dog studied with a fluorescent antibody.. Doctor of Philosophy Thesis. Wayne State University; Detroit, Michigan: 1961
    Google Scholar
  • 7 Lewis M. L, Ware A. G. A simple procedure for separation of prothrombin and accelerator globulin from citrated human plasma.. Proc. Soc. exp. Biol. (N.Y.) 1953; 84: 636
    CrossrefPubMedGoogle Scholar
  • 8 Nordschow C. D, Robinson J. N, Carter J. R. Personal communication. Iowa State University; Iowa City, Iowa.:
    Google Scholar
  • 9 Seegers W. H. The purification of prothrombin.. Rec. Chem. Prog. 1952; 13: 143
    PubMedGoogle Scholar
  • 10 Kabat E. A, Mayer M. M. Experimental Immunochemistry. Charles C. Thomas Springfield; Illinois: 1948
    Google Scholar
  • 11 Grabar P, Williams C. A. Méthode permettant l’étude conjuguée des propriétés électrophorétiques et immunochimiques d’un mélange de protéines. Application au sérum sanguin.. Biochim. biophys. Acta 1953; 10: 193
    CrossrefPubMedGoogle Scholar
  • 12 Wilson M. W, Pringle B. H. Experimental studies of the agar plate precipitin test of Ouchterlony.. J. Immunol. 1954; 73: 232
    PubMedGoogle Scholar
  • 13 Wilson M. W. Experimental records. Medical Library, Wayne State University, Detroit, Michigan. 1958 1957
    Google Scholar
  • 14 Goodman M, Ramsey D. S, Simpson W. L, Remp D. G, Ba-sinski D. H, Brennan M. J. The use of chicken antiserum for the rapid determination of plasma protein components.. J. Lab. clin. Med. 1957; 49: 151
    PubMedGoogle Scholar
  • 15 Seegers W. H, Casillas G, Shepard R. S, Thomas W. R, Halick P. Some properties of thrombin preparations.. Canad. J. Biochem. 1959; 37: 775
    CrossrefPubMedGoogle Scholar
  • 16 Scheiffarth F, Götz H, Soergel K. Immunoelektrophoretische Studien über heterologe Präzipitinreaktionen.. Int. Arch. Allergy 1957; 10: 82
    CrossrefPubMedGoogle Scholar
  • 17 Melcher L. R, Masouredis S. P, Reed R. The immunological relationship between human and bovine serum albumin.. J. Immunol. 1953; 70: 125
    PubMedGoogle Scholar
  • 18 Vigliani E. C, Pernis B. Immunological factors in the pathogenesis of the hyaline tissue of Silicosis.. Brit. J. industr. Med. 1958; 15: 8
    PubMedGoogle Scholar
  • 19 Farr R. S, Dixon Jr. F. J. The effect of antigen concentration on the initiation of detectable antibody synthesis in rabbits.. J. Immunol. 1960; 85: 250
    PubMedGoogle Scholar
  • 20 Schwick G, Schultze H. E. Immunchemische Untersuchungen mit Prothrombin und Thrombin. Colloq. Sint. Jans Hospital, Brügge, Belgien, 1958.. Clin. chim. Acta 1959; 4: 26
    CrossrefPubMedGoogle Scholar