Ren, S <br/><br/>
Human tryptase fibrinogenolysis is optimal at acidic pH and generates anticoagulant fragments in the presence of the anti-tryptase monoclonal antibody B12.  [electronic resource] 

 -  Journal of immunology (Baltimore, Md. : 1950)  Oct 1997 
 - 3540-8 p.  digital 
<br/><br/> Publication Type: Journal Article; Research Support, U.S. Gov't, P.H.S. 
<br/><br/><label>ISSN: </label>0022-1767 
<br/><br/><label>Subjects--Topical Terms: </label><br/>Adjuvants, Immunologic--pharmacology<br/>Antibodies, Monoclonal--metabolism<br/>Binding, Competitive--immunology<br/>Catalysis<br/>Chymases<br/>Dextran Sulfate<br/>Drug Stability<br/>Fibrinogen--immunology<br/>Fibrinolysin--metabolism<br/>Fibrinolysis--immunology<br/>Humans<br/>Hydrogen-Ion Concentration<br/>Hypersensitivity, Immediate--metabolism<br/>Male<br/>Middle Aged<br/>Oligopeptides--immunology<br/>Peptide Fragments--immunology<br/>Serine Endopeptidases--immunology<br/>Serine Proteinase Inhibitors--immunology<br/>Skin Tests<br/>Substrate Specificity<br/>Tryptases