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Q28366837-4AFE12A5-ED30-4617-BE20-EC51D647C63C
Q28366837-4AFE12A5-ED30-4617-BE20-EC51D647C63C
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http://www.wikidata.org/entity/statement/Q28366837-4AFE12A5-ED30-4617-BE20-EC51D647C63C
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
Q28366837-4AFE12A5-ED30-4617-BE20-EC51D647C63C
BestRank
Statement
http://www.wikidata.org/entity/statement/Q28366837-4AFE12A5-ED30-4617-BE20-EC51D647C63C
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wasDerivedFrom
b4d4e7bbaca88a14b1bc494e22cc537aa3515c21
P2860
Steady state kinetic evidence for an acyl-enzyme intermediate in reactions catalyzed by bovine spleen cathepsin B.