Origin of human triosephosphate isomerase isozymes: further evidence for the single structural locus hypothesis with Japanese variants.
Four electrophoretic variants 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 (1981) 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. (1981) that both the isozyme e and TPI-A are deamidation products of TPI-B.
D002238:Carbohydrate Epimerases / Q000235:genetics*; D002455:Cell Division; D002874:Chromosome Mapping; D004591:Electrophoresis, Polyacrylamide Gel; D004912:Erythrocytes / Q000166:cytology / Q000201:enzymology*; D005796:Genes; D005819:Genetic Markers; D006801:Humans; D007527:Isoenzymes / Q000097:blood / Q000235:genetics*; D007564:Japan; D008214:Lymphocytes / Q000166:cytology / Q000201:enzymology; D011110:Polymorphism, Genetic; D014305:Triose-Phosphate Isomerase / Q000097:blood / Q000235:genetics*
D005819:Genetic Markers; D007527:Isoenzymes; D002238:Carbohydrate Epimerases; D014305:Triose-Phosphate Isomerase