Human Glyoxalase Research Articles

85] Glyoxalase I from human erythrocytes

Glyoxalase I catalyzes the formation of S-2-hydroxyacylglutathione from 2-oxoaldehydes, such as methylglyoxal and glutathione (GSH). This chapter describes the assay method, the purification procedure, and the properties of glyoxalase I isolated from human erythrocytes. Human glyoxalase I exists in the form of three isozymes that appear identical in their functional properties. The increase in absorbance at 240 nm because of thiolester formation from glutathione (GSH) and methylglyoxal is monitored spectrophotometrically. The purification procedure involves denaturation of hemoglobin, acetone fractionation, ammonium sulfate fractionation, affinity chromatography (I) on S-Hexylglutathione-Sepharose 6B, chromatography on Sephadex G-75, affinity chromatography II, chromatography on diethylaminoethyl (DEAE)-Sepharose, and separation of isozymes of glyoxalase I. The enzyme obtained by this procedure appears homogeneous as judged by various analytical procedures, except for the presence of the three isozymes. The enzyme is composed of two subunits of equal weight and contains one Zn per subunit that is essential to catalytic activity.

Assignment of the glyoxalase II gene (HAGH) to human chromosome 16.

The human and rodent forms of glyoxalase II (Hydroxyacylglutathione hydrolase, HAGH) can readily be separated by starch gel electrophoretic procedures. Fifty-one human-rodent somatic cell hybrid clones were examined for their human HAGH and for human enzyme markers whose genes are encoded on each autosome and the X chromosome. Sixteen clones were also examined for their human karyotypes. Human glyoxalase II segregated only with chromosome 16, demonstrating that the gene is located on this chromosome.

Human red glyoxalase I polymorphism in the Swiss population: phenotype frequencies and a simplified technique.

A simple, cheap and rapid electrophoresis technique for the separation and detection of red cell glyoxalase is described. Frequency of GLO I1 is 0.444 and of GLO I2 0.556 respect

Rapid detection of glyoxalase I (GLO) on cellulose acetate gel and the distribution of GLO variants in a Dutch population.

A rapid electrophoretic procedure is described for detecting the human red cell glyoxalase I variants (GLO 1, GLO 2-1, and GLO 2) on cellulose acetate gel (cellogel) on which the sites of enzymed activity are visualized as purple bands against white background. The frequency of GLO1 gene in a Dutch population living in and around Leiden was found to be 0.4544.

Possible assignment of the glyoxalase I (GLO) gene to chromosome 6 using man-mouse somatic cell hybrids.

A correlation between the expression or absence of human glyoxalase I and chromosome 6 (as well its markers ME1, IPO-B, and PGM3) was observed in man-mouse somatic cell hybrids. This segregation pattern indicates that the GLO gene is situated on chromosome 6.

Assignment of the genes for human glyoxalase I to chromosome 6 and for human esterase D to chromosome 13

Assignment of the genes for human glyoxalase I to chromosome 6 and for human esterase D to chromosome 13