Advertisement
Paper| Volume 37, ISSUE 6, P681-688, March 15, 1985

Acceleration of fibrin gel formation by unrelated proteins

  • Jacob Wilf
    Affiliations
    Laboratory of Biochemical Pharmacology, National Institute of Arthritis, Diabetes, and Digestive and Kidney Diseases, National Institutes of Health, Building 4, Room B1-27, Bethesda, Maryland 20205 USA
    Search for articles by this author
  • Jules A. Gladner
    Affiliations
    Laboratory of Biochemical Pharmacology, National Institute of Arthritis, Diabetes, and Digestive and Kidney Diseases, National Institutes of Health, Building 4, Room B1-27, Bethesda, Maryland 20205 USA
    Search for articles by this author
  • Allen P. Minton
    Affiliations
    Laboratory of Biochemical Pharmacology, National Institute of Arthritis, Diabetes, and Digestive and Kidney Diseases, National Institutes of Health, Building 4, Room B1-27, Bethesda, Maryland 20205 USA
    Search for articles by this author
      This paper is only available as a PDF. To read, Please Download here.

      Abstract

      Addition of γ-globulin, serum albumin, hemoglobin, or ovalbumin in concentrations of 1–10 g/dl to solutions of purified fibrinogen results in a substantial (up to six-fold) decrease in the lag time preceding appearance of a firm fibrin gel following addition of thrombin at 24°C. The effect does not appear to be due to a protein-induced enhancement in the enzymatic activity of thrombin, nor does it appear to be due to the co-condensation of the added protein with fibrin/fibrinogen. It is suggested that the observed effect is primarily due to nonspecific volume exclusion arising from increased fractional occupancy of solution volume by macromolecules.

      Keywords

      To read this article in full you will need to make a payment

      Purchase one-time access:

      Academic & Personal: 24 hour online accessCorporate R&D Professionals: 24 hour online access
      One-time access price info
      • For academic or personal research use, select 'Academic and Personal'
      • For corporate R&D use, select 'Corporate R&D Professionals'

      Subscribe:

      Subscribe to Thrombosis Research
      Already a print subscriber? Claim online access
      Already an online subscriber? Sign in
      Institutional Access: Sign in to ScienceDirect

      References

      1. Jamieson G.A. Greenwalt T Blood Substitutes and Plasma Expanders. Alan R. Liss, New York1978
        • Alexander B.
        Effects of plasma expanders on coagulation and hemostasis.
        in: Jamieson G.A. Greenwalt T Blood Substitutes and Plasma Expanders. Alan R. Liss, New York1978: 293-326
        • Minton A.P.
        The effect of volume occupancy upon the thermodynamic activity of proteins: Some biochemical consequences.
        Mol. Cell. Biochem. 1983; 55: 119-140
        • Laurent T.C.
        The interaction between polysaccharides and other macromolecules.
        Biochem. J. 1963; 89: 253-257
        • Minton K.W.
        • Karmin P.
        • Rahn G.M.
        • Minton A.P.
        Non-specific stabilization of stress-susceptible proteins by stress-resistant proteins.
        in: Proc. Natl. Acad. Sci. U.S.A.79. 1982: 7107-7111
        • Gladner J.A.
        • Folk J.E.
        • Laki K.
        • Carroll W.R.
        Thrombin-induced formation of co-fibrin. I. Isolation, purification and characterization of co-fibrin.
        J. Biol. Chem. 1959; 234: 62-66
        • Folk J.E.
        • Gladner J.A.
        • Laki K.
        Thrombin-induced formation of co-fibrin. II. Preliminary amino acid sequence studies on peptides A and B.
        J. Biol. Chem. 1959; 234: 67-70
        • Irreverre F.A.
        A modified Sakaguchi spray.
        Biochim. Biophys. Acta. 1965; 111: 551-552
        • Alexander B.
        • Odaka K.
        • Lawlor D.
        • Swanger M.
        Coagulation, hemostasis and plasma expanders: A quarter-century enigma.
        in: Fed. Proc.34. 1975: 1429-1440
        • Minton A.P.
        Non-ideality and the thermodynamics of sickle-cell hemoblogin gelation.
        J. Mol. Biol. 1977; 110: 89-103
        • Minton A.P.
        Excluded volume as a determinant of macromolecular structure and reactivity.
        Biopolymers. 1981; 20: 2093-2120