Purification and characterization of two forms of glyoxalase II from the liver and brain of wistar rats

Principato, Giovanni; Rosi, Gabriella; Talesa, Vicenzo; Giovanni, Elvio; Uotila, Lasse

doi:10.1016/0167-4838(87)90076-8

Cited by 158 publications

(69 citation statements)

References 11 publications

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“…From experiments on specific chemical modification resulting in inactivation of the glyoxalase II enzyme, it was proposed that histidine, arginine (or lysine), and aspartic acid (or glutamic acid) residues are required for the function of glyoxalase II (1,41,42). Each of these residues can be found in one or more of the conserved boxes, especially three histidine residues are totally conserved in box II (TH-H-DH).…”

Section: Discussionmentioning

confidence: 99%

Identification and Phenotypic Analysis of Two Glyoxalase II Encoding Genes from Saccharomyces cerevisiae,GLO2 and GLO4, and Intracellular Localization of the Corresponding Proteins

Bito

Haider

Hadler

et al. 1997

Journal of Biological Chemistry

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We have isolated and characterized two genes coding for the glyoxalase II enzyme from Saccharomyces cerevisiae. The coding region of the GLO2 gene corresponds to a protein with 274 amino acids and a molecular mass of 31,306 daltons. The open reading frame of the GLO4 gene could be translated into a protein with 285 amino acids and a molecular mass of 32,325 daltons. The amino acid sequences of the deduced proteins are 59.1% identical and show high similarities to the sequence of the human glyoxalase II. When grown on either glucose or glycerol as a carbon source, a glo2 glo4 double deletion strain contains no glyoxalase II activity at all and shows no obvious phenotype during vegetative growth. However, this strain showed a similar high sensitivity against exogenous methylglyoxal as compared with a glyoxalase I-deficient strain. Whereas the GLO2 gene is expressed on both glucose and glycerol, the GLO4 gene is only active on glycerol. The active Glo2p protein is localized in the cytoplasm and the active Glo4p in the mitochondrial matrix. Heterologous expression of the full-length GLO2 coding region in Escherichia coli resulted in an active protein. However, to get an active Glo4p protein in E. coli, the putative mitochondrial transit peptide at the N-terminal end had to be removed by shortening the 5 end of the GLO4 open reading frame.

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Section: Discussionmentioning

confidence: 99%

Identification and Phenotypic Analysis of Two Glyoxalase II Encoding Genes from Saccharomyces cerevisiae,GLO2 and GLO4, and Intracellular Localization of the Corresponding Proteins

Bito

Haider

Hadler

et al. 1997

Journal of Biological Chemistry

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“…In rat liver, 10-15 % of total glyoxalase II activity is in the mitochondria. The cytosolic enzyme consists of two forms of molecular mass 17 and 29 kDa, and pI values between 7.4 and 8.1 (Principato et al, 1987b;Talesa et al, 1988) (Table 2).…”

Section: Glyoxalase IImentioning

confidence: 99%

The glyoxalase system: new developments towards functional characterization of a metabolic pathway fundamental to biological life

Thornalley

1990

Biochemical Journal

732

502

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“…Glyoxalase I (GI, EC 4.4.1.5) activity was determined according to ORAY and NORTON (1977) at 240 nm (ε = 3.37 mM -1 cm -1 ) using 1.5 mM GSH/methylglyoxal hemithioacetal as substrate. Glyoxalase II (GII, EC 3.1.2.6) was determined according to PRINCIPATO et al (1987) at 412 nm (ε = 13.6 mM -1 cm -1 ) by monitoring GSH formation in the presence of 5,5′-dithio-bis-2-nitrobenzoic acid (DTNB) and S-D-lactoylglutathione (LSG). Protein concentration of supernatant fractions was determined according to LOWRY et al (1951) employing bovine serum albumin (BSA) as a protein standard.…”

Section: Biochemical Analysismentioning

confidence: 99%

Glutathione and Antioxidant Enzymes in the Hepatopancreas of Crayfish Procambarus Clarkii (Girard, 1852) of Lake Trasimeno (Italy)

Elia

Dörr

Mastrangelo

et al. 2006

Bull. Fr. Pêche Piscic.

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Antioxidant parameters, such as total glutathione, glutathione S-transferase, glutathione peroxidase, glutathione reductase, glyoxalases, catalase, and some heavy metals such as, lead, cadmium and chromium were examined in hepatopancreas of both sexes of Procambarus clarkii collected seasonally from Lake Trasimeno, from winter 2000-2003 to autumn 2003. Heavy metals content in hepatopancreas in males and females of P. clarkii was low and did not vary through the sampling periods and between sexes. On the contrary, crayfish exhibited sex-dependent differences in levels of some enzyme activities and of total glutathione, and no apparent relationship was found between contaminant burdens and antioxidant indexes in hepatopancreas. Because measured metal concentrations were low, other factors, presumably, were involved in antioxidant variations in P. clarkii and these latter seemed to be affected more by biological and environmental factors, other than those related to pollutants body burdens.

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Purification and characterization of two forms of glyoxalase II from the liver and brain of wistar rats

Cited by 158 publications

References 11 publications

Identification and Phenotypic Analysis of Two Glyoxalase II Encoding Genes from Saccharomyces cerevisiae,GLO2 and GLO4, and Intracellular Localization of the Corresponding Proteins

Identification and Phenotypic Analysis of Two Glyoxalase II Encoding Genes from Saccharomyces cerevisiae,GLO2 and GLO4, and Intracellular Localization of the Corresponding Proteins

The glyoxalase system: new developments towards functional characterization of a metabolic pathway fundamental to biological life

Glutathione and Antioxidant Enzymes in the Hepatopancreas of Crayfish Procambarus Clarkii (Girard, 1852) of Lake Trasimeno (Italy)

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