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Journal of Pharmacology And Experimental Therapeutics, Vol. 189, Issue 2, 544-549, 1974
Copyright © 1974 by American Society for Pharmacology and Experimental Therapeutics

KINETICS OF SUCCINYLDITHIOCHOLINE HYDROLYSIS BY SERUM CHOLINESTERASE: COMPARISON TO DIBUCAINE AND SUCCINYLCHOLINE NUMBERS

Louis B. Hersh 1, P. Prithvi Raj 1, and David Ohlweiler 1

1 Department of Biochemistry and the Department of Anesthesiology, The University of Texas Southwestern Medical School, Dallas, Texas

Succinyldithiocholine was utilized as substrate analog of succinyldicholine to study the kinetic properties of normal and atypical serum cholinesterase (EC. 3.1.1.8). The normal serum cholinesterase has a mean Km of 0.032 mM for succinyldithiocholine hydrolysis. On the other hand, the enzyme from individuals classified as heterozygous or homozygous with respect to atypical serum cholinesterase exhibit considerably higher mean Km values, 0.097 and 1.08 mM, respectively. In all three classes, little, if any, difference is noted in the maximal rate of succinyldithiocholine hydrolysis. Both dibucaine and succinylcholine number appears to correlate with Km for succinyldithiocholine.

Submitted on November 15, 1973
Accepted on January 31, 1974






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Copyright © 1974 by the American Society for Pharmacology and Experimental Therapeutics.