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J. Biochem, 1977, Vol. 81, No. 5 1393-1399
© 1977 Japanese Biochemical Society

research-article

Affinity Labeling of Adenine Nucleotide-Related Enzymes with Reactive Adenine Nucleotide Analogs

II. Affinity Labeling of Phosphoglycerate Kinase with a Reactive AMP Analog

Koichi SUZUKI, Chikahiko EGUCHI1 and Kazutomo IMAHORI

Department of Biochemistry, Faculty of Medicine, The University of Tokyo Bunkyo-ku, Tokyo 113

Affinity labeling of yeast and B. stearothermophilus phosphoglycerate kinases with a reactive AMP analog, N6-(p-bromoacetaminobenzyl)-AMP was examined. Complete loss of enzyme activity was observed when 1 mol of the reagent had reacted per mol of either enzyme. Results on the effect of pH and substrate addition on the inactivation, titration of SH groups before and after modification, and kinetic studies with AMP analogs suggest that the modification occurs at one amino group at or near the subtrate binding site. General affinity labeling of kinases is discussed based on the results obtained.

1Present address Central Research Laboratories, Ajinomoto Co., Inc., Kawasaki-ku, Kawasaki 210.


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