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]
Producer: 19841119Description: 805-14 p. digitalISSN:- 0264-6021
- 2,2'-Dipyridyl -- analogs & derivatives
- Animals
- Arginine -- analogs & derivatives
- Benzoylarginine-2-Naphthylamide -- analogs & derivatives
- Binding Sites
- Cathepsin B
- Cathepsins -- metabolism
- Cattle
- Disulfides
- Humans
- Hydrolysis
- Indicators and Reagents -- metabolism
- Kinetics
- Liver -- enzymology
- Models, Chemical
- Pyridines -- metabolism
- Rats
- Species Specificity
- Spleen -- enzymology
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Publication Type: Comparative Study; Journal Article; Research Support, Non-U.S. Gov't
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