Abstract
Two families segregating for the atypical (E1a) allele at cholinesterase locus 1 are described. Unusual results for dibucaine inhibition led to the recognition of a new allele (E1k) also segregating in these families. The enzymatic and immunological data are consistent with the hypothesis that E1k causes reduction of 'usual' (E1u) molecules by about 33%. Whether the reduction of E1u caused by E1k is caused by retarded synthesis or accelerated degradation of serum cholinesterase remains to be determined.
Highlights
Several quantitative variants at serum cholinesterase (E.C.3.1.1.8) locus 1 have been described. These result in lowered serum cholinesterase activity and, when interacting with the E,a allele, give dibucaine inhibitions below those of E,UE,a heterozygotes
We present here two families with a quantitative variant at cholinesterase locus 1 which results in about 33% reduction of E,u molecules; both of these families were recognised by means of interaction with the E, a gene
The cholinesterase activities and inhibitions of the sera of the family members are giveni in the Table
Summary
The enzymatic and immunological methods used were the same as given in earlier publications (Garry et al, 1976; Rubinstein et al, 1976; Dietz et al, 1973). (Table II in Garry et al (1976) gives the cholinesterase activities and inhibitions of the known phenotypes as determined in our laboratory.)Received for publication 30 May 1977. The enzymatic and immunological methods used were the same as given in earlier publications (Garry et al, 1976; Rubinstein et al, 1976; Dietz et al, 1973). (Table II in Garry et al (1976) gives the cholinesterase activities and inhibitions of the known phenotypes as determined in our laboratory.).
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