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Q28366837-633FAEFD-8DE8-4DC9-95E0-51B92E168CAB
Q28366837-633FAEFD-8DE8-4DC9-95E0-51B92E168CAB
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http://www.wikidata.org/entity/statement/Q28366837-633FAEFD-8DE8-4DC9-95E0-51B92E168CAB
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
P2860
Q28366837-633FAEFD-8DE8-4DC9-95E0-51B92E168CAB
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Statement
http://www.wikidata.org/entity/statement/Q28366837-633FAEFD-8DE8-4DC9-95E0-51B92E168CAB
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b4d4e7bbaca88a14b1bc494e22cc537aa3515c21
P2860
Half-time analysis of the integrated Michaelis equation. Simulation and use of the half-time plot and its direct linear variant in the analysis of some alpha-chymotrypsin, papain- and fumarase-catalysed reactions.