The Journal of Biochemistry
Online ISSN : 1756-2651
Print ISSN : 0021-924X
Purification of Fibrinogen Using Cationic Detergent
Susumu KURIOKAFumihide INOUEFukuichi NAKADA
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1975 年 77 巻 2 号 p. 457-461

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Stearyltrimethylammonium chloride was used to isolate human fibrinogen, and purified protein was obtained by removing the detergent bound to it. Medium consisting of 0.015-0.03mM fibrinogen-detergent complex, 0.85M NaCl, 0.03M sodium caprylate, and 30% ethanol was found to be effective for renaturation of fibrinogen from the complex. The purified fibrinogen did not form any fibrils on incubation for 15 days with Ca+2 at pH 7.2, and 37° The clottability of the purified fibrinogen was over 99%. Immunochemical studies showed that the purified fibrinogen produced one precipitation line with a mixture of anti-human fibrinogen and anti-human serum. Although highly purified, the fibrinogen preparation still contained a trace of plasminogen.

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