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Journal ArticleDOI

S-carbobenzoxyglutathione: a competitive inhibitor of mammalian glyoxalase II.

Y. R. Hsu, +1 more
- 01 Dec 1983 - 
- Vol. 26, Iss: 12, pp 1784-1785
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TLDR
S-Carbobenzoxyglutathione has found utility as an affinity ligand for the purification of rat liver glyoxalase II, and it may well have use in the study of the gly oxalase enzymes in vivo.
Abstract
An effective competitive inhibitor of mammalian glyoxalase II has been synthesized and studied. The compound, S-carbobenzoxyglutathione, is almost totally inactive as an inhibitor of mammalian glyoxalase I. This is in marked contrast to other glyoxalase II competitive inhibitors, which in general are even more effective against glyoxalase I. S-Carbobenzoxyglutathione has found utility as an affinity ligand for the purification of rat liver glyoxalase II, and it may well have use in the study of the glyoxalase enzymes in vivo.

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Book ChapterDOI

Methylglyoxal and Regulation of its Metabolism in Microorganisms

TL;DR: The complexity of the regulation of metabolism of methyl glyoxal implies that the glycolytic methylglyoxal pathway is not only a detoxification system in cells, but also may have some significant functions in the characteristic properties of living systems—that is growth, proliferation, and differentiation.
Journal ArticleDOI

Purification and characterisation of glyoxalase II from human red blood cells.

TL;DR: S-p-Nitrobenzoxycarbonylglutathione was a potent competitive inhibitor of glyoxalase II with a Ki value of 1.20 +/- 0.21 microM, and the hemithioacetal formed non-enzymically from the reaction of methylglyoxal with reduced glutathionewas a weak competitive inhibitor with a ki value of 834 +/- 98 microM.
Journal ArticleDOI

Demonstration of glyoxalase II in rat liver mitochondria. Partial purification and occurrence in multiple forms.

TL;DR: Results give evidence for the presence of mitochondrial glyoxalase II which is different from the cytosolic enzymes in several characteristics.
Journal ArticleDOI

A simplified method for the purification of human red blood cell glyoxalase. I. Characteristics, immunoblotting, and inhibitor studies

TL;DR: The polyclonal antibodies were raised to the purified enzyme and were found to react specifically with glyoxalase I antigen by immunoblotting and gave a protein of high purity with simple low pressure chromatographic techniques with a moderate but adequate yield for small-scale preparations.
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