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Chemical characterization of a new Japanese variant of carbonic anhydrase I, CA INagasaki 1(76 Arg→Gln)

✍ Scribed by Kazuaki Goriki; Richard E. Tashian; Sharon K. Stroup; Ya-Shiou L. Yu; Dag M. Henriksson

Publisher
Springer
Year
1979
Tongue
English
Weight
514 KB
Volume
17
Category
Article
ISSN
0006-2928

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✦ Synopsis

A new inherited variant of carbonic anhydrase I (CA I), designated CA INagasaki 1 (CA INGS 1), was discovered during a survey of hemolysates from 5852 individuals from the cities of Hiroshima and Nagasaki in Japan. Analysis of the amino acid composition of a tryptic peptide from the CA INGS 1 variant indicated that a glutaminyl residue was substituted for an arginyl residue at position 76. Heat degradation studies showed that the CA INGS 1 variant was less stable than normal CA I. The CO2 hydrase and esterase activities of the normal and variant carbonic anhydrases I, as well as the relative amounts of the two enzymes in heterozygotes, were similar.

📜 SIMILAR VOLUMES

Amino acid substitution and chemical cha
Amino acid substitution and chemical characterization of a Japanese variant of carbonic anhydrase I: CA I Hiroshima-1 (86 Asp → Gly)
✍ Takeshi Kageoka; David Hewett-Emmett; Sharon K. Stroup; Ya-Shiou L. Yu; Richard 📂 Article 📅 1981 🏛 Springer 🌐 English ⚖ 675 KB

An electrophoretic variant of red cell carbonic anhydrase L 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