Purification and cloning of glyoxalase II from rat liver

Glyoxalase (GLO) II, which is a component of GLO system and catalyze the conversion of S-lactoyl-glutathione to D-lactate, was purified 1488 fold from rat liver by two steps of Affigel blue and carbobenzoxyglutathione-Sepharose 4B affinity chromatography. The molecular weight of the enzyme was estim...

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Bibliographic Details
Published in:Experimental & molecular medicine 1998-03, Vol.30 (1), p.53-57
Main Authors: Cho, M Y, Bae, C D, Park, J B, Lee, T H
Format: Article
Language:English
Subjects:
Amino Acid Sequence
Animals
Base Sequence
Cloning, Molecular
Liver - enzymology
Molecular Sequence Data
Rats
Rats, Sprague-Dawley
Sequence Analysis, DNA
Sequence Homology, Amino Acid
Thiolester Hydrolases - genetics
Thiolester Hydrolases - isolation & purification
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Summary:Glyoxalase (GLO) II, which is a component of GLO system and catalyze the conversion of S-lactoyl-glutathione to D-lactate, was purified 1488 fold from rat liver by two steps of Affigel blue and carbobenzoxyglutathione-Sepharose 4B affinity chromatography. The molecular weight of the enzyme was estimated to be 29 kDa which is similar to those from other species. The sequence of N-terminal 9 amino acid residues was determined to be MGIRLLPAT. This was then used to synthesize degenerative primers. cDNA clone was isolated by first synthesizing cDNA from RNA and then PCR amplification. The sequence of cDNA clone was determined by serial sequencing analysis.
ISSN:1226-3613
2092-6413
2092-6413
DOI:10.1038/emm.1998.8