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Further studies on D-3-aminoisobutyrate-pyruvate aminotransferase.
Ueno, S; Sano, A; Hineno, T; Kondoh, K; Mizuno, T; Morino, H; Kakimoto, Y.
Afiliação
  • Ueno S; Department of Neuropsychiatry, Ehime University School of Medicine, Japan.
Biochim Biophys Acta ; 1035(2): 128-31, 1990 Aug 17.
Article em En | MEDLINE | ID: mdl-2393662
D-3-Aminoisobutyrate-pyruvate aminotransferase (EC 2.6.1.40, D-BAIB aminotransferase) participates in the metabolism of thymine. Recently we purified this enzyme from rat liver. We have studied D-BAIB aminotransferase further to clarify its physiological function. Among our findings were the following. (1) The enzyme activity was widely distributed in the organs of guinea pigs and rats. The kidney, liver, and lung showed high specific activities. (2) Using the livers of six vertebrates, differences between species were studied. Activity was detected in all species, the human liver showing the lowest activity among them. (3) Developmental study using rat liver showed that the activity was low at birth, increased sharply thereafter for 10 days, and then subsequently declined to the adult level. (4) Intraperitoneal injection of BAIB and beta-alanine in rats was performed to determine whether they induce activity of this aminotransferase. Only BAIB increased the activity of the aminotransferase in the liver significantly. (5) Subcellular distribution study of this aminotransferase in rat liver revealed that it is a mitochondrial enzyme.
Assuntos
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Coleções: 01-internacional Base de dados: MEDLINE Assunto principal: Transaminases / Fígado Limite: Animals / Humans Idioma: En Revista: Biochim Biophys Acta Ano de publicação: 1990 Tipo de documento: Article País de afiliação: Japão
Buscar no Google
Coleções: 01-internacional Base de dados: MEDLINE Assunto principal: Transaminases / Fígado Limite: Animals / Humans Idioma: En Revista: Biochim Biophys Acta Ano de publicação: 1990 Tipo de documento: Article País de afiliação: Japão