Purification and cloning of glyoxalase II from rat liver
Experimental & Molecular Medicine
;
: 53-57, 1998.
Artigo
em Inglês
| WPRIM
| ID: wpr-192956
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.
Texto completo:
DisponíveL
Índice:
WPRIM (Pacífico Ocidental)
Assunto principal:
Tioléster Hidrolases
/
Estudo Comparativo
/
Dados de Sequência Molecular
/
Sequência de Bases
/
Sequência de Aminoácidos
/
Clonagem Molecular
/
Homologia de Sequência de Aminoácidos
/
Análise de Sequência de DNA
/
Ratos Sprague-Dawley
/
Fígado
Limite:
Animais
Idioma:
Inglês
Revista:
Experimental & Molecular Medicine
Ano de publicação:
1998
Tipo de documento:
Artigo
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