Willenbrock, F <br/><br/>
Natural structural variation in enzymes as a tool in the study of mechanism exemplified by a comparison of the catalytic-site structure and characteristics of cathepsin B and papain. pH-dependent kinetics of the reactions of cathepsin B from bovine spleen and from rat liver with a thiol-specific two-protonic-state probe (2,2'-dipyridyl disulphide) and with a specific synthetic substrate (N-alpha-benzyloxycarbonyl-L-arginyl-L-arginine 2-naphthylamide).  [electronic resource] 

 -  The Biochemical journal  Sep 1984 
 - 805-14 p.  digital 
<br/><br/> Publication Type: Comparative Study; Journal Article; Research Support, Non-U.S. Gov't 
<br/><br/><label>ISSN: </label>0264-6021 
<br/><br/><label>Standard No.: </label>10.1042/bj2220805  doi 
<br/><br/><label>Subjects--Topical Terms: </label><br/>2,2'-Dipyridyl--analogs & derivatives<br/>Animals<br/>Arginine--analogs & derivatives<br/>Benzoylarginine-2-Naphthylamide--analogs & derivatives<br/>Binding Sites<br/>Cathepsin B<br/>Cathepsins--metabolism<br/>Cattle<br/>Disulfides<br/>Humans<br/>Hydrolysis<br/>Indicators and Reagents--metabolism<br/>Kinetics<br/>Liver--enzymology<br/>Models, Chemical<br/>Pyridines--metabolism<br/>Rats<br/>Species Specificity<br/>Spleen--enzymology