Abstract |
Incubation of normal human plasma or its euglobulin fraction with chloroform enhances the generation of proteolytic activity attributable to plasmin. The mechanisms involved remain unclear. Earlier, plasmin formation was found to be impaired in the chloroform-treated euglobulin fraction of Hageman trait plasma. We now demonstrate sharply reduced generation of fibrinolytic and caseinolytic activities in prekallikrein-deficient (Fletcher trait) and HMW kininogen-deficient ( Fitzgerald trait) plasmas as well. These defects were corrected by addition of the missing factors. In addition, precipitation of the euglobulin fraction of plasma activated small but measurable amounts of HF. With the use of 125I-HF, cleavage of the native molecule into its amino-terminal and carboxy-terminal fragments occurred pari passu with the generation of plasmin. These experiments suggest that one pathway through which HF can bring about formation of plasmin in chloroform-treated euglobulin fractions involves the participation of plasma prekallikrein and HMW kininogen, presumably through mechanisms similar to those evoked by surface activation of HF.
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Authors | E M Gordon, O D Ratnoff, G H Goldsmith Jr |
Journal | The Journal of laboratory and clinical medicine
(J Lab Clin Med)
Vol. 95
Issue 4
Pg. 507-14
(Apr 1980)
ISSN: 0022-2143 [Print] United States |
PMID | 7359011
(Publication Type: Journal Article, Research Support, U.S. Gov't, P.H.S.)
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Chemical References |
- Caseins
- Kininogens
- Serum Globulins
- Chloroform
- Factor XII
- Prekallikrein
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Topics |
- Animals
- Caseins
(physiology)
- Cattle
- Chloroform
(pharmacology)
- Electrophoresis, Polyacrylamide Gel
- Factor XII
- Fibrinolysis
(drug effects)
- Humans
- Kininogens
- Molecular Weight
- Prekallikrein
- Serum Globulins
(physiology)
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