Protease nexin. Properties and a modified purification procedure.
نویسندگان
چکیده
منابع مشابه
Protease nexin. Properties and a modified purification procedure.
The present paper describes chemical and functional properties of protease nexin, a serine protease inhibitor released from cultured human fibroblasts. It is shown that protease nexin is actually synthesized by fibroblasts and represents about 1% of their secreted protein. Analysis of the amino acid composition of purified protease nexin indicates that it is evolutionarily related to antithromb...
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This paper describes a simple purification procedure for protease nexin, a serine proteinase inhibitor secreted by cultured human fibroblasts that regulates proteinase activity at and near the cell surface. The first step in the procedure takes advantage of the high-affinity binding of protease nexin to dextran sulphate-Sepharose. This step eliminates the need for prior concentration of the ser...
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Protease nexin-1 (PN-1) is a serpin that inhibits plasminogen activators, plasmin, and thrombin. PN-1 is barely detectable in plasma but is expressed by platelets. Here, we studied platelet PN-1 in resting and activated conditions and its function in thrombosis. Studies on human platelets from healthy donors and from patients with a Gray platelet syndrome demonstrate that PN-1 is present both a...
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A mast cell protease has been purified over 260-fold from rat thyroid homogenates. The purified enzyme hydrolyzes denatured thyroglobulin, denatured hemoglobin, and fibrinogen. It also rapidly hydrolyzes the ester substrates, benzoyltyrosine ethyl ester, benzoylphenylalanine ethyl ester, and acetyltyrosine ethyl ester. The pH optimum for thyroglobulin and benzoyltyrosine ethyl ester hydrolysis ...
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Penicilliurn expamum grown in a medium with rice husk as a carbon source produced an extracellular protease. The protease enzyme was isolated from culture broth by fractionation with acetone and column chromatography on Sephadex G- 100 and DEAE A-50. The protease enzyme was purified about 17.47 fold, with a recovery of 14%. The purified protease was homogenous on SDS polyacrylarnide disc ge...
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ژورنال
عنوان ژورنال: Journal of Biological Chemistry
سال: 1985
ISSN: 0021-9258
DOI: 10.1016/s0021-9258(18)88883-4