Literature DB >> 117793

Chemical characterization of a new Japanese variant of carbonic anhydrase I, CA INagasaki 1 (76 arg leads to gln).

K Goriki, R E Tashian, S K Stroup, Y S Yu, D M Henriksson.   

Abstract

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.

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Year:  1979        PMID: 117793     DOI: 10.1007/bf00498883

Source DB:  PubMed          Journal:  Biochem Genet        ISSN: 0006-2928            Impact factor:   1.890


  23 in total

1.  Widespread distribution of variant forms of carbonic anhydrase in Australian aboriginals.

Authors:  N M Blake; R L Kirk
Journal:  Med J Aust       Date:  1978-02-25       Impact factor: 7.738

2.  Human carbonic anhydrases. XI. The complete primary structure of carbonic anhydrase B.

Authors:  K T Lin; H F Deutsch
Journal:  J Biol Chem       Date:  1973-03-25       Impact factor: 5.157

3.  Biochemical characterization of the human carbonic anhydrase variant CA Ih Hiroshima.

Authors:  R J Tanis; W R Osborne; N Ueda; R E Tashian
Journal:  Hum Genet       Date:  1976-09-10       Impact factor: 4.132

4.  Crystal structure of human erythrocyte carbonic anhydrase B. Three-dimensional structure at a nominal 2.2-A resolution.

Authors:  K K Kannan; B Notstrand; K Fridborg; S Lövgren; A Ohlsson; M Petef
Journal:  Proc Natl Acad Sci U S A       Date:  1975-01       Impact factor: 11.205

5.  Human carbonic anhydrases. XII. The complete primary structure of the C isozyme.

Authors:  K T Lin; H F Deutsch
Journal:  J Biol Chem       Date:  1974-04-25       Impact factor: 5.157

6.  The detection and differentiation of the products of the human carbonic anhydrase loci, CAI and CAII using fluorogenic substrates.

Authors:  D A Hopkinson; J S Coppock; M F Mühlemann; Y H Edwards
Journal:  Ann Hum Genet       Date:  1974-10       Impact factor: 1.670

7.  Carbonic anhydrase isozymes in Cavia porcellus, Cavia aperea and their hybrids.

Authors:  N D Carter
Journal:  Comp Biochem Physiol B       Date:  1972-11-15

8.  Primary structure of human carbonic anhydrase C.

Authors:  L E Henderson; D Henriksson; P O Nyman
Journal:  J Biol Chem       Date:  1976-09-25       Impact factor: 5.157

9.  The frequency in Japanese of genetic variants of 22 proteins II. Carbonic anhydrase I and II, lactate dehydrogenase, malate dehydrogenase, nucleoside phosphorylase, triose phosphate isomerase, haemoglobin A and haemoglobin A2.

Authors:  N Ueda; C Satoh; R J Tanis; R E Ferrell; S Kishimoto; J V Neel; H B Hamilton; K Baba
Journal:  Ann Hum Genet       Date:  1977-07       Impact factor: 1.670

10.  Thermal inactivation studies of normal and variant human erythrocyte carbonic anhydrases by using a sulphonamide-binding assay.

Authors:  W R Osborne; R E Tashian
Journal:  Biochem J       Date:  1974-07       Impact factor: 3.857

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  3 in total

1.  Human erythrocyte carbonic anhydrase polymorphism in Kenya.

Authors:  A Kendall
Journal:  Hum Genet       Date:  1979-11       Impact factor: 4.132

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

Authors:  T Kageoka; D Hewett-Emmett; S K Stroup; Y S Yu; R E Tashian
Journal:  Biochem Genet       Date:  1981-06       Impact factor: 1.890

3.  A polymorphic variant of human erythrocyte carbonic anhydrase I with a widespread distribution in Australian aborigines, CAI Australia-9 (8 Asp leads to Gly): purification, properties, amino acid substitution, and possible physiological significance of the variant enzyme.

Authors:  G L Jones; D C Shaw
Journal:  Biochem Genet       Date:  1982-10       Impact factor: 1.890

  3 in total

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