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Abstract

Several advantages of basing analyses of steady state kinetics of allosteric enzymes on Linkage principles are pointed out; among them the ease and exactness of tests that can be applied to the data of limited accuracy normally available. These advantages are illustrated by some analyses of the allosteric kinetics of dCMP aminohydrolase (EC 3.5.4.12). Some of the allosteric interactions analyzed are known to have a role in controlling mutation rates in mammalian cells.

Additional information

Authors: WHITEHEAD E P CEC BRUXELLES (BELGIUM) AND UNIVERISITA DI ROMA (ITALY), CEC BRUXELLES (BELGIUM) AND UNIVERISITA DI ROMA (ITALY)
Bibliographic Reference: BIOCHEMICAL DYNAMICS, NATO ADVANCED WORKSHOP, MARSEILLE (FRANCE), SEPT. 18-23, 1983 WRITE TO CEC LUXEMBOURG, DG XIII/A2, POB 1907 MENTIONING PAPER E 31281 ORA
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