Technical Report No. 8-85
Origin of human triosephosphate isomerase isozymes: Further evidence for the single structural locus hypothesis with Japanese variants
Asakawa J, Iida SEditor’s note: A publication based on this report was published in Hum Genet 70:222-30, 1985.
Summary
Four electrophoretic vairants of human erythrocyte triosephosphate isomerase (TPI) have been studied to investigate the origin of the multiple forms of human TPI, in particular the constitutive TPI-B isozyme and the cell division-associated TPI-A isozyme. The variant phenotype expressed by the constitutive TPI-B isozyme in both erythrocytes and peripheral lymphocytes was also expressed by the cell division-associated isozymes in mitogen-stimulated lymphocytes and hair-root cells. These results strongly support the hypothesis of Decker and Mohrenweiser that TPI-B and TPI-A originated from the same structural gene. We also found that the isozyme e is different from TPI-A with respect to both its electrophoretic mobility and heat stability. This finding is in contrast to the recent conclusion of Yuan et al that both the isozyme e and TPI-A are deamidation products of TPI-B.
Four electrophoretic vairants of human erythrocyte triosephosphate isomerase (TPI) have been studied to investigate the origin of the multiple forms of human TPI, in particular the constitutive TPI-B isozyme and the cell division-associated TPI-A isozyme. The variant phenotype expressed by the constitutive TPI-B isozyme in both erythrocytes and peripheral lymphocytes was also expressed by the cell division-associated isozymes in mitogen-stimulated lymphocytes and hair-root cells. These results strongly support the hypothesis of Decker and Mohrenweiser that TPI-B and TPI-A originated from the same structural gene. We also found that the isozyme e is different from TPI-A with respect to both its electrophoretic mobility and heat stability. This finding is in contrast to the recent conclusion of Yuan et al that both the isozyme e and TPI-A are deamidation products of TPI-B.