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Q28366837-BB2605D5-D2B7-4458-8BC1-FF7DDA630915
Q28366837-BB2605D5-D2B7-4458-8BC1-FF7DDA630915
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Statement
http://www.wikidata.org/entity/statement/Q28366837-BB2605D5-D2B7-4458-8BC1-FF7DDA630915
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-BB2605D5-D2B7-4458-8BC1-FF7DDA630915
BestRank
Statement
http://www.wikidata.org/entity/statement/Q28366837-BB2605D5-D2B7-4458-8BC1-FF7DDA630915
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wasDerivedFrom
b4d4e7bbaca88a14b1bc494e22cc537aa3515c21
P2860
Evidence for a two-state transition in papain that may have no close analogue in ficin. Differences in the disposition of cationic sites and hydrophobic binding areas in the active centres of papain and ficin.