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Q28366837-02AAAFAC-36FA-4666-9D8E-FE3C117E8D5A
Q28366837-02AAAFAC-36FA-4666-9D8E-FE3C117E8D5A
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http://www.wikidata.org/entity/statement/Q28366837-02AAAFAC-36FA-4666-9D8E-FE3C117E8D5A
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
Q28366837-02AAAFAC-36FA-4666-9D8E-FE3C117E8D5A
BestRank
Statement
http://www.wikidata.org/entity/statement/Q28366837-02AAAFAC-36FA-4666-9D8E-FE3C117E8D5A
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wasDerivedFrom
b4d4e7bbaca88a14b1bc494e22cc537aa3515c21
P2860
Differences in the interaction of the catalytic groups of the active centres of actinidin and papain. Rapid purification of fully active actinidin by covalent chromatography and characterization of its active centre by use of two-protonic-state reac