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Extra resources for Affinity labeling
Karpeisky, S. Mora, E. I. Okina, and L. V. Yudina, Eur. J. Biochem. 40, 519 (1973). K. Pfister, J. H. R. I~gi, and P. Christen, Experientia 32) 773 (1976).  SYNC&TALYTIC ENZYME MODIFICATION 45 Interference of Syncatalytic Modification with Affinity Labeling and Differentiation of the Two Types of Enzyme Labeling Although differing in mechanism, syncatalytic modification and affinity labeling have one feature in common: the simultaneous interaction of the enzyme with a substrate moiety and with a reagent moiety.
Indeed, the enzyme was 1~W. Birchmeier and P. Christen, J. Biol. Chem. 249, 6311 (1974). 14M. Okamoto and Y. Morino, J. Biol. Chem. 248, 82 (1973). 46 GENERAL M~THODOLOGY  found to be inactivated by bromopyruvate only in the presence of amino acid cosubstrates, such as glutamate. , 2-ketoglutarate in concentrations of up to 50 times Kin) failed to inhibit inactivation by bromopyruvate, the latter being used in a concentration of 3 times Kin. Apparently, attachment of bromopyruvate to the substrate binding site is not a prerequisite for inactivation to occur.
Terry, Arch. Biochem. Biophys. 160, 135 (1974). ° J. O. Westerik and R. Wolfenden, J. Biol. Chem. 247, 8195 (1971). P R. C. Thompson, Biochemistry 12, 47 (1973). J. O. Westerik a n d R . Wolfenden, J. Biol. Chem. 249, 6351 (1974). r j. D. Findlater and B. A. Orsi, FEBS Left. $6, 109 (1973) ° J. Conchie, A. J. Hay, I. Strachan, and G. A. Levvy, Biochem. J. 102, 929 (1967). t It. L. Lai and B. Axelrod, Biochem. Biophys. Res. Commun. 64, 463 (1973). B. E. Evans and R. Wolfenden, J. Am. Chem. Soc. 92, 4751 (1970).