Amino acid substitution and chemical characterization of a Japanese variant of carbonic anhydrase I: CA I Hiroshima-1 (86 Asp ? Gly)

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Abstract
An electrophoretic variant of red cell carbonic anhydrase I, designated CA I Hiroshima-1, has been observed in 12 apparently unrelated individuals during a survey of 13,019 individuals from the cities of Hiroshima and Nagasaki, Japan. Analyses of tryptic and chymotryptic peptide patterns of this CA I variant purified from 8 of the 12 individuals revealed the same altered peptides in each case. Examination of the amino acid sequence of an altered tryptic peptide purified from one of the variants showed that the aspartic acid residue at position 86 was replaced by a glycine residue. Thermostability studies demonstrated that all samples of CA I Hiroshima-1 were less stable than normal CA I. The specific esterase (p-nitrophenyl acetate) activities of the normal and variant CA I isozymes were essentially the same. The difference spectra of the normal and variant enzymes were essentially the same. The isoelectric focusing patterns of CA I Hiroshima-1 showed a different pattern of minor bands to those produced by normal CA I. The relative amounts of the normal and variant enzymes purified from single heterozygous individuals were similar.