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Characterization of two new electrophoretic variants of human triosephosphate isomerase: Stability, kinetic, and immunological properties

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Abstract

Two new electrophoretic variants of human triosephosphate isomerase (TPI) have been partially purified and characterized. The TPI Manchester variant, a cathodally migrating electrophoretic allozyme identified in an individual with the phenotype TPI 1-Manchester, is associated with a normal level of enzyme activity in erythrocytes and normal kinetic properties. It is very thermolabile at 55 and 57° C, although it is not uniquely sensitive to either guanidine-HCl or urea denaturation. The TPI Hiroshima-2 variant is an anodally migrating allozyme (the phenotype of proband is TPI 1-Hiroshima-2) with normal activity and kinetic properties and also normal stability characteristics. It is inactivated less by antisera raised against normal human TPI than either the normal or the Manchester allozyme. Dissociation-reassociation experiments utilizing these allozymes have confirmed that normal human red blood cell TPI isozymes are produced by a sequence of reactions (presumably deamidations) involving alternating subunits.

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Author notes

  1. J. Asakawa

    Present address: Radiation Effects Research Foundation, 730, Hiroshima, Japan

Authors and Affiliations

  1. Department of Human Genetics, University of Michigan Medical School, 48109, Ann Arbor, Michigan

    J. Asakawa & H. W. Mohrenweiser

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  1. J. Asakawa
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  2. H. W. Mohrenweiser
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Financial support was derived from Contract EY-77-C-02-2828 from the Department of Energy.

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Asakawa, J., Mohrenweiser, H.W. Characterization of two new electrophoretic variants of human triosephosphate isomerase: Stability, kinetic, and immunological properties. Biochem Genet 20, 59–76 (1982). https://doi.org/10.1007/BF00484936

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  • DOI: https://doi.org/10.1007/BF00484936

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