Characterization of two new electrophoretic variants of human triosephosphate isomerase: stability, kinetic, and immunological properties.
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 degrees 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.
D000937:Antigen-Antibody Reactions; D002238:Carbohydrate Epimerases / Q000235:genetics*; D004591:Electrophoresis, Polyacrylamide Gel; D004912:Erythrocytes / Q000201:enzymology; D014644:Genetic Variation; D006801:Humans; D066298:In Vitro Techniques; D007527:Isoenzymes / Q000235:genetics / Q000302:isolation & purification* / Q000378:metabolism; D007700:Kinetics; D014305:Triose-Phosphate Isomerase / Q000235:genetics* / Q000276:immunology / Q000378:metabolism; D014306:Trioses
D007527:Isoenzymes; D014306:Trioses; D002238:Carbohydrate Epimerases; D014305:Triose-Phosphate Isomerase