Two affinity chromatography methods for the purification of glyoxalase I from rabbit liver

Elango, N.; Janaki, S.; Rao, A.R.

doi:10.1016/0006-291x(78)91375-x

Cited by 15 publications

(6 citation statements)

References 14 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…In this system, coupling of matrix and ligand occurs via spacer and amino-groups of the ligand. Other affinity matrices -S-hexyl-GSH-coupled agarose, blue dextran Sepharose -which have been used in the purification of animal glyoxalase gave no positive result (Elango et al 1978;Rhee et al 1986; Baskaran and Absorption ( ) was measured at 280 nm. The specific fraction eluted at 16.2-16.3 h (Gly I) was identified as glyoxalase I by two different activity assays (native gels and spectrophotometrically).…”

Section: Correlation Of Glyoxalase-i Activity With Cell Proliferationmentioning

confidence: 99%

Physiological and biochemical characterization of glyoxalase I, a general marker for cell proliferation, from a soybean cell suspension

Paulus

Köllner

Jacobsen

1993

Planta

View full text Add to dashboard Cite

Using a strictly auxin-dependent soybean (Glycine max (L.) Merr.) cell suspension, we studied the correlation of auxin-dependent cell proliferation and the activity of glyoxalase I (S-lactoylglutathione-lyase EC 4.4.1.5), and enzyme generally associated with cell proliferation in animal, microbial and, as reported recently, also plant systems. We found the activity of glyoxalase I to be modulated during the proliferation cycle, with a maximal activity between day 2 and day 4 of culture growth. After starving the culture of auxins for three subsequent periods, both the enzyme activity and cell-growth could be re-initiated with auxin. Enzyme activity reached its maximum 1 d before cell number was at a maximum. The enzyme was purified to homogeneity and characterized.

show abstract

Section: Correlation Of Glyoxalase-i Activity With Cell Proliferationmentioning

confidence: 99%

Physiological and biochemical characterization of glyoxalase I, a general marker for cell proliferation, from a soybean cell suspension

Paulus

Köllner

Jacobsen

1993

Planta

View full text Add to dashboard Cite

show abstract

“…of 43000 for glyoxalase I from mouse liver was determined by ultracentrifugation (Kester & Norton, 1975). Other values for mammalian glyoxalase I were estimated by gel filtration: sheep liver, 45900 (Uotila & Koivusalo, 1975), rat erythrocytes and rat liver, 50000 (Han et al, 1976), and rabbit liver, 42000 (Elango et al, 1978). Thus the microbial glyoxalase I molecules (mol.wts.…”

Section: Physical Properties Ofglyoxalase Imentioning

confidence: 99%

Comparison of glyoxalase I purified from yeast (Saccharomyces cerevisiae) with the enzyme from mammalian sources

Marmstål

Aronsson

Mannervik

1979

Biochemical Journal

View full text Add to dashboard Cite

Glyoxalase I from yeast (Saccharomyces cerevisiae) purified by affinity chromatography on S-hexylglutathione-Sepharose 6B was characterized and compared with the enzyme from rat liver, pig erythrocytes and human erythrocytes. The molecular weight of glyoxalase I from yeast was, like the enzyme from Rhodospirillum rubrum and Escherichia coli, significantly less (approx. 32000) than that of the enzyme from mammals (approx. 46000). The yeast enzyme is a monomer, whereas the mammalian enzymes are composed of two very similar or identical subunits. The enzymes contain 1Zn atom per subunit. The isoelectric points (at 4 degrees C) for the yeast and mammalian enzymes are at pH7.0 and 4.8 respectively; tryptic-peptide ;maps' display corresponding dissimilarities in structure. These and some additional data indicate that the microbial and the mammalian enzymes may have separate evolutionary origins. The similarities demonstrated in mechanistic and kinetic properties, on the other hand, indicate convergent evolution. The k(cat.) and K(m) values for the yeast enzyme were both higher than those for the enzyme from the mammalian sources with the hemimercaptal adduct of methylglyoxal or phenylglyoxal as the varied substrate and free glutathione at a constant and physiological concentration (2mm). Glyoxalase I from all sources investigated had a k(cat.)/K(m) value near 10(7)s(-1).m(-1), which is close to the theoretical diffusion-controlled rate of enzyme-substrate association. The initial-velocity data show non-Michaelian rate saturation and apparent non-linear inhibition by free glutathione for both yeast and mammalian enzyme. This rate behaviour may have physiological importance, since it counteracts the effects of fluctuations in total glutathione concentrations on the glyoxalase I-dependent metabolism of 2-oxoaldehydes.

show abstract

“…S -Alkylglutathiones play various functions in living organisms. For instance, S -alkylglutathiones act as selective ligands of brain ionotropic glutamate receptors, are inhibitors of the glyoxylase cycle, , and protect glutathione transferase from inactivation . In addition, S -Me-Glu acts as an inhibitor of the reduction of S -nitrosoglutathione mediated by alcohol dehydrogenase, albeit substitution of the sulfhydryl proton in GSH with a methyl group hardly improved the inhibitory effect of GSH by itself .…”

Section: Introductionmentioning

confidence: 99%

Sensitized Photooxidation of S-Methylglutathione in Aqueous Solution: Intramolecular (S∴O) and (S∴N) Bonded Species

et al. 2013

View full text Add to dashboard Cite

Nanosecond laser flash photolysis was used to generate sulfur radical cations of the thioether, S-methylglutathione (S-Me-Glu), via the one-electron oxidation of this thioether by triplet 4-carboxybenzophenone. The purpose of this investigation was to follow the neighboring group effects resulting from the interactions between the sulfur radical cationic sites and nearby lone-pair electrons on heteroatoms within the radical cation, especially the electron lone-pairs on heteroatoms in the peptide bonds. The tripeptide, S-Me-Glu, offers several possible competing neighboring group effects that are characterized in this work. Quantum yields of the various radicals and three-electron bonded (both intramolecular and intermolecular) species were determined. The pH dependence of photoinduced decarboxylation yields was used as evidence for the identification of a nine-membered ring, sulfur-nitrogen, three-electron bonded species. The mechanisms of the secondary reactions of the radicals and radical cations were characterized by resolving their overlapping transient-absorption spectra and following their kinetic behavior. In particular, sulfur-oxygen and sulfur-nitrogen three-electron bonded species were identified where the oxygen and nitrogen atoms were in the peptide bonds.

show abstract

Two affinity chromatography methods for the purification of glyoxalase I from rabbit liver

Cited by 15 publications

References 14 publications

Physiological and biochemical characterization of glyoxalase I, a general marker for cell proliferation, from a soybean cell suspension

Physiological and biochemical characterization of glyoxalase I, a general marker for cell proliferation, from a soybean cell suspension

Comparison of glyoxalase I purified from yeast (Saccharomyces cerevisiae) with the enzyme from mammalian sources

Sensitized Photooxidation of S-Methylglutathione in Aqueous Solution: Intramolecular (S∴O) and (S∴N) Bonded Species

Contact Info

Product

Resources

About