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By Silvio Garattini

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The patient was also resistant to dicoumarol and the indanedione anticoagulant phenindione, but not to heparin. The degree of binding of warfarin to the patient’s plasma proteins was identical to that of normal subjects. Electrophoretic studies showed that warfarin was bound exclusively to albumin, as in normal plasma. Warfarin was not excreted unchanged in urine or stools, even after administration of very high doses. A metabolite of warfarin was recovered from the patient’s urine in amounts similar to those recovered from the urine of normal subjects given equivalent amounts of drug.

Wilson (1954)had previously described two sites on cholinesterase molecules, an anionic site which accommodated the positively charged choline radical of the substrate and an esteratic site into which the acid portion of the substrate was positioned during hydrolysis. Recent work of Clark et al. (1968) demonstrated that the pK of the atypical enzyme is lower than that of the usual enzyme, that choline alters the pK of the usual but not of the atypical enzyme, and that choline has a lower affinity for the atypical enzyme.

Close resemblance of most populations in their gene frequencies of atypical pseudocholinesterase implies that little selective advantage is conferred now by the various genotypes or that the pertinent environmental conditions are similar in widely different countries. , 1958) shown by Harris and Whittaker (1962b)to be the glycoalkaloid solanine. Since atypical pseudocholinesterase is less sensitive to inhibition by this naturally occurring substance than is the normal enzyme, it has been suggested that in cases of solanine poisoning the atypical genotype would be a t a selective advantage.

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