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DOI: 10.1055/s-0038-1654841
The Effect of Sulfhydrylinhibitors and Glycine Derivatives on Fibrin Polymerization and the Physical Strength of Fibrin in Plasma
Publication History
Publication Date:
22 June 2018 (online)

Summary
The influence of p-CMB, iodoacetamide, iodoacetic acid, N-ethylmaleimide, glycerinederivatives and of EDTA on thrombingeneration on fibrinpolymeriza- tion and on the physical strength of clots as expressed by spectrophotometrical and thrombelastographic measurements respectively has been examined.
P-CMB and N-ethylmaleimide significantly inhibit the thrombin generation.
EDTA retards the initial steps of the fibrinpolymerization and it increases the final turbidity. Its effect is neutralized by calcium and magnesium. The sulfhydrylinhibitors do not inhibit the polymerization neither do the glycinederivatives.
To judge from these results does FSF not influence the polymerization but calcium and magnesium do. This statement is verified using FSF deficient plasma.
The four SH-inhibitors tested inhibit the development of a normal thromb- elastogram, specially in reducing the mA values. Cysteine, having no effect by itself, reverses the effect of p-CMB and iodoacetamide.
p-CMB has a similar effect when added to FSF deficient plasma and the main effect of this SH inhibition is suggested to be on platelet enzymes. p-CMB and iodoacetic acid also reduce the m A values of platelet-free normal plasma possibly by inhibiting FSF.
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References
- 1 Astrup T. Biochemistry of blood coagulation. Acta physiol, scand.. Suppl. 21. 1944
- 2 Beck E, Duckert F, Ernst M. The influence of fibrin stabilizing factor on the growth of fibroblasts in vitro and wound healing. Thrombos. Diathes. haemorrh. (Stuttg) 06: 485 1961;
- 3 Ferry J. D, Miller M, Shumann S. The conversion of fibrinogen to fibrin. VII rigidity and stress relaxation of fibrin clots, effect of calcium. Arch. Biochem. 34: 424 1951;
- 4 Ferry J. D, Morrison P. R. Preparations and properties of serum and plasma proteins: VIII The conversion of human fibrinogen under various conditions. J. Amer. chem. Soc. 69: 388 1947;
- 5 Gormsen J. Studies on Heparin Tolerance Test. Acta haemat. (Basel) 24: 213 1960;
- 6 Gormsen J, Fletcher A. P. Relationship between clot structural parameters and thrombolysis. Fed. Proc. 22: 2400 1963;
- 7 Gormsen J, Fletcher A. P, Alkjaersig N, Sherry S. In praep..
- 8 Hartert H. Die Thrombelastographie. Z. exp. Med. 117: 189 1951;
- 9 Katz S, Shulman S, Tinoco I, Billick I. H, Gutfreund K, Ferry J. D. The Conversion of fibrinogen to fibrin XIV. The effect of calcium on the formation and dissociation of intermediate polymers. Arch. Biochem. 47: 165 1953;
- 10 Laki K, Lorand L. On the solubility of fibrin clots. Science 108: 280 1948;
- 11 Loewy A. G, Dunathan K, Gallant J. A, Gardner B. Fibrinase III. Some enzymatic properties. J. biol. Chem. 236: 2644 1961;
- 12 Loewy A. G, Gallant J. A, Dunathan K. Fibrinase IV. Effect on fibrin solubility. J. biol. Chem. 236: 2648 1961;
- 13 Lorand L. Fibrino-peptide: new aspects of the fibrinogen-fibrin transformation. Nature (Lond) 167: 992 1951;
- 14 Lorand L. Properties and significance of the fibrin stabilizing factor (FSF). Thrombos. Diathes. haemorrh. (Stuttg). Suppl. 1 and VII, 238. 1962
- 15 Lorand L, Koniski K, Jacobsen A. Transpeptidation mechanism in blood clotting. Nature (Lond) 194: 1148 1962;
- 16 Löhr G. W, Waller H. D, Groß E. Beziehungen zwischen dem Plättchenstoffwechsel und der Retraction des Blutgerinnsels. Dtsch. med. Wschr. 86 897, 949 1961;
- 17 Rosenfeld G, Jauszky B. The accelerating effect of calcium on the fibrinogen-fibrin transformation. Science 116: 36 1952;
- 18 Scheraga H. A. Protein structure. Academic Press; New York: 1961
- 19 Scheraga H. A, Laskowski Jr M. Advances in protein chemistry. Academic Press, New York. XII: 1 1957;
- 20 Steiner R. F, Laki K. Light scattering studies on the clotting of fibrinogen. Arch. Biochem. 34: 24 1951;