Absence of Blood Clotting Substances from Synovial Fluid^[*]

Summary

Analyses were performed on normal bovine synovial fluid for prothrombin, fibrinogen, Ac-globulin (factor V), autoprothrombin I (factor VII), tissue thromboplastin, and antithrombin. None of these active substances in blood clotting was found. The absence of these proteins, especially prothrombin (MW of 62 700), may be on the basis of selective permeability of the capillaries of the synovial membrane to certain plasma proteins.

^* This study was supported by grant A-532 (C11) of the United States Public Health Service, and by the Michigan Chapter, Arthritis and Rheumatism Foundation.

• References

• 1 Ropes M. W, Bauer W. Synovial fluid changes in joint disease. 39 Harvard University Press; Cambridge: 1953
• 2 Schmid K, MacNair M. B. Characterization of the proteins of certain postmortem human synovial fluids. J. clin. Invest 37: 708 1958;
• 3 Neuhaus O. W, Letzring M. Hexosamine-containing glycoproteins of normal bovine synovial fluid. J. biol. Chem 232: 177 1958;
• 4 Decker B, McKenzie B. F, McGuckin W. F. Zone electrophoretic studies of proteins and glycoproteins of bovine serum and synovial fluid. Proc. Soc. exp. Biol. (N. Y) 102: 616 1959;
• 5 Ropes M. W, Bennett G. A, Bauer W. The origin and nature of normal synovial fluid. J. clin. Invest 18: 357 1939;
• 6 Lamy F, Waugh D. F. Certain physical properties of bovine prothrombin. J. biol. Chem 203: 489 1953;
• 7 Laki K, Kominz D. R, Symonds P, Lor L, Seegers W. H. The amino acid composition of bovine prothrombin. Arch. Biochem. Biophys 49: 276 1954;
• 8 Seegers W. H, McClaughry R. I, Fahey J. L. Some properties of purified prothrombin and its activation with sodium citrate. Blood 05: 421 1950;
• 9 Landaburu R. Personal communication.
• 10 Seegers W. H, Alkjaersig N, Johnson S. A. On the nature of the blood coagulation mechanisms in certain clinical states. Amer. J. clin. Path 25: 983 1955;
• 11 Ware A. G, Seegers W. H. Two-stage procedure for the quantitative determination of prothrombin concentration. Amer. J. clin. Path 19: 471 1949;
• 12 Seegers W. H, Smith F. I. P. Factors which influence the activity of purified thrombin. Amer. J. Physiol 137: 348 1942;
• 13 Abul-Haj S. K, Watson J, Rinehart J. F, Page E. W. The thrombo- plastic activity of hyaluronate. Science 114: 237 1951;
• 14 Sylvén B. in “The Biochemistry and Physiology of Bone”. 57 Bourne G. H. (Ed.), Academic Press, Inc; New York: 1956
• 15 Wolfson W. Q, Cohn C, Calvary E, chib F. I. Studies in serum proteins. V. A rapid procedure for the estimation of total protein, true albumin, total globulin, alpha globulin, beta globulin and gamma globulin in 1.0 ml of serum. Amer. J. clin. Path 18: 723 1948;
• 16 Tocantins L. M. (Ed.): The Coagulation of Blood. 124 Grune and Stratton; New York: 1955
• 17 ibid., p. 144.
• 18 Carter J. R, Warner E. D. Quantitative estimation of plasma accelerator globulin. Proc. Soc. exp. Biol. (N. Y) 75: 223 1950;
• 19 McClaughry R. I, Seegers W. H. Prothrombin, thromboplastin, Ac-globulin and platelet accelerator: Quantitative interrelationships. Blood 05: 303 1950;
• 20 Seegers W. H, Miller K. E, Andrews E. B, Murphy R. C. Fundamental interactions and effect of storage, ether, adsorbants and blood clotting on plasma antithrombin activity. Amer. J. Physiol 169: 700 1952;