Gene/Protein Disease Symptom Drug Enzyme Compound
Pivot Concepts:   Target Concepts:
Query: EC:3.4.21.7 (plasmin)
 9,023 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Synthetic humic acid, well water humic acid and commercial humic acid (Aldrich) all have the ability to inhibit human plasmin activity. At a concentration of 20 micrograms/ml, all three species will result in 93%, 70% and 40% of residual plasmin activity, respectively. The components of humic acid, such as protocatechuic acid, resorcinol, vanillic acid and ferulic acid do not have such inhibitory activities. The ability of humic acid to inhibit human plasmin has not been reported. It is, therefore, a new plasmin inhibitor.
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PMID:Humic acid: inhibitor of plasmin. 153 19

SOLUBILIZED PROTEIN DERIVED FROM HUMAN PLATELETS WAS FRACTIONATED BY DEAE CELLULOSE COLUMN CHROMATOGRAPHY AND ANALYZED FOR PROTEASE ACTIVITY USING THREE SUBSTRATES: denatured bovine hemoglobin, alpha casein, and purified plasminogen-free human fibrinogen. A protein fraction was found with proteolytic activity which was heat labile and not attributable to plasmin. The activity was not potentiated by cysteine or inhibited by iodoacetamide. Studies of pH optima indicated a broad range of enzyme activity with peaks in both the acid and alkaline region. Cathepsin A activity was detected in the platelet protease fraction by hydrolysis of the synthetic substrate N-carbobenzoxy-alpha-L-glutamyl-L-tyrosine. Similar proteolytic activity was found when the proteins derived from isolated platelet granules were examined. The results indicate that human platelets possess potent intracellular proteolytic enzymes. The relationship of this proteolytic activity to the hemostatic process is discussed.
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PMID:Studies on human platelet protease activity. 423 82