Purification of S-2-hydroxyacylglutathione hydrolase (glyoxalase II) from rat erythrocytes

Glyoxalase II, a specific glutathione thiolesterase, has been purified 9100-fold from rat erythrocytes using a purification scheme which employs Affi-Gel blue as a hydrophobic affinity column and also employs a glutathione-affinity column prepared by coupling S-( p-chlorophenacyl)glutathione to Affi...

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Bibliographic Details
Published inAnalytical biochemistry Vol. 98; no. 2; pp. 472 - 477
Main Authors Ball, James C., Vander Jagt, David L.
Format Journal Article
LanguageEnglish
Published United States Elsevier Inc 01.10.1979
Subjects
Animals
Chromatography, Affinity - methods
Chromatography, Ion Exchange - methods
Erythrocytes - enzymology
Glutathione Transferase - blood
Glutathione Transferase - isolation & purification
Rats
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Summary:Glyoxalase II, a specific glutathione thiolesterase, has been purified 9100-fold from rat erythrocytes using a purification scheme which employs Affi-Gel blue as a hydrophobic affinity column and also employs a glutathione-affinity column prepared by coupling S-( p-chlorophenacyl)glutathione to Affi-Gel 202. This procedure offers a convenient method for the preparation of highly purified glyoxalase II. Also described is a convenient method for the preparation of S-lactoyl-glutathione, a substrate for glyoxalase II.
Bibliography:ObjectType-Article-1
SourceType-Scholarly Journals-1
ObjectType-Feature-2
content type line 23
ISSN:0003-2697
1096-0309
DOI:10.1016/0003-2697(79)90169-6