von Deimling_1981_Biochem.Genet_19_1091

A polymorphism for an isozyme of a presumed arylesterase, esterase-16 (EC 3.1.1.2), has been detected in kidney, heart, and spleen of the house mouse, Mus musculus, by means of isoelectric focusing and by disc electrophoresis. Three phenotypes can be distinquished: the ES-16A phenotype (IEP 5.9) was found in C57BL/10Sn and many other laboratory inbred strains; the ES-16B phenotype (IEP 6.1) was found in M. m. molossinus; and the ES-16C phenotype (IEP 5.9; very weak activity) was found in Peru-Coppock. Esterase-16 is strongly inhibited by 10(-3) M p-chloromercuribenzoate, but not by 2. 10(-4) M bis-p-nitrophenyl phosphate or by 10(-3) M Diamox. It stains well with indoxyl acetate and other indigogenic substrates but only weakly with alpha-naphthyl acetate. Esterase-16 is completely insoluble in water. It is apparently governed by a structural gene locus, Es-16, with three alleles, Es-16a, Es-16b, and ES-16c, respectively. Es-16 is closely linked to Car-1 and Car-2 on chromosome 3 Typing of 94 animals of the backcross (C57BL/10Sn x M. m. mol.) F1 x M. m. mol. revealed a recombination frequency of 8.51 /+- 2.9%.