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Immobilized Polyelectrolyte Enzyme Systems. Activation of Polyornithylchymotrypsin by the Product of the Enzymic Reaction
Author(s) -
Goldstein Leon
Publication year - 1973
Publication title -
israel journal of chemistry
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.908
H-Index - 54
eISSN - 1869-5868
pISSN - 0021-2148
DOI - 10.1002/ijch.197300036
Subject(s) - chemistry , propionate , tyrosine , polyelectrolyte , sulfonate , hydrolysis , enzyme , medicinal chemistry , derivative (finance) , stereochemistry , organic chemistry , biochemistry , sodium , polymer , financial economics , economics
The hydrolysis of N‐acetyl‐ L ‐tyrosine ethyl ester catalyzed by a polycationic derivative of chymotrypsin, polyornithylchymotrypsin (POCH), was studied in the presence of varying concentrations of N‐acetyl‐ L ‐tyrosine, the product of the enzymic reaction. The values of k cat (lim) and K m (app) for polyornithylchymotrypsin increased hyperbolically with increasing concentrations of N‐acetyl‐ L ‐tyrosine. Increase in the values of k cat (lim) and K m (app) of polyornithylchymotrypsin was also observed in the presence of other organic anions, e.g. acetate, propionate, benzoate and l‐anilino‐8‐naphthalene sulfonate. The hyperbolic dependence of k cat (lim) and K m (app) of polyornithylchymotrypsin on the concentration of N‐acetyl‐ L ‐tyrosine suggested that the data could be treated as a saturation phenomenon. The activation of polyornithylchymotrypsin could be attributed to the cancellation of charge resulting from the binding of organic anions to the positively charged side chains of the enzyme derivative.