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Apparent kinetic constants inhibition studies

From the kinetic study o/lb-catalyzed hydrolysis of 4-nitrophenyl acetate inhibited by various aromatic sulfonamides, the apparent 1 1 affinity constants were determined at jH 8.4/ A comparison o/intramolecular Kntra=10 =Wor ll)/i (for la)]ond intermolecular for la with / toluenesulfonamide) contribution of p-toluenesulfonamide anion coordination to the zinc(II)-[12]aneN3 complex gives an effective mo-larity M by the intramolecular location. [Pg.182]


See other pages where Apparent kinetic constants inhibition studies is mentioned: [Pg.133]    [Pg.23]    [Pg.284]    [Pg.284]    [Pg.494]    [Pg.174]    [Pg.290]    [Pg.793]    [Pg.794]    [Pg.173]    [Pg.489]    [Pg.283]    [Pg.299]    [Pg.245]    [Pg.393]    [Pg.26]    [Pg.1722]    [Pg.474]    [Pg.374]    [Pg.350]   
See also in sourсe #XX -- [ Pg.83 ]




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