Purification and cloning of glyoxalase II from rat liver.
- Author:
Mi Young CHO
1
;
Chang Dae BAE
;
Jae Bong PARK
;
Tong Ho LEE
Author Information
1. Department of Biochemistry, Medical College, Hallym University.
- Publication Type:Original Article ; Comparative Study ; Research Support, Non-U.S. Gov't
- Keywords:
glyoxalase II;
liver;
purification;
sequence
- MeSH:
Amino Acid Sequence;
Animal;
Base Sequence;
Cloning, Molecular;
Comparative Study;
Liver/enzymology*;
Molecular Sequence Data;
Rats;
Rats, Sprague-Dawley;
Sequence Analysis, DNA;
Sequence Homology, Amino Acid;
Thiolester Hydrolases/isolation & purification;
Thiolester Hydrolases/genetics
- From:Experimental & Molecular Medicine
1998;30(1):53-57
- CountryRepublic of Korea
- Language:English
-
Abstract:
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.
