Studies on Protein Fractions Isolated from Human Plasma

Autor: B. S. Combridge, Elsie Silk, Brenda Mason, Margaret E. Mackay
Rok vydání: 1970
Předmět:
Zdroj: British Journal of Haematology. 18:29-44
ISSN: 1365-2141
0007-1048
DOI: 10.1111/j.1365-2141.1970.tb01416.x
Popis: Summary. Fractions of human plasma separated by precipitation with cold ether and ethanol were examined for a number of protease and esterase activities. Plasminogen, kallikrein, increased vascular permeability, thrombin and TAMe esterase were concentrated in fraction G2/iR, a lipo-protein fraction containing a mixture of alpha and beta globulins and a gamma-M globulin, which also contained activated coagulation contact factors. ATEe esterase was concentrated in G2/iR and fibrinogen. Kinin-ase and TAMe esterase were also found in G2/2 a mixture of alpha, beta and gamma globulins. Tests of fractions of G2/iR separated by chromatography confirmed the findings of Kagen et al, (1963) and showed that kallikrein was a gamma-M globulin. Vascular permeability activity, but not kininogenase activity was removed by high-speed centrifugation from this fraction. Fractions G2/iR, G2/2 and to a lesser extent G3 contained a substance which induced kininogenase activation in intact plasma, but was not identified as PF, plasmin or activated contact factor and had no esterase activity. Kininogenase activity was associated with contaminants of fibrinogen and gamma globulin concentrates and absent from albumin. In fractions prepared by large-scale methods, only those made from G2 are likely to contain sufficient kininogenase to cause a clinical reaction. Kininogenase was not adsorbed by Al(OH)3 gel or Ca3(PO4)2 and would not contaminate clotting factors prepared from G2.
Databáze: OpenAIRE
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