Alanine aminotransferase and glycine aminotransferase from maize [Zea mays L.] leaves

• Autorzy: Orzechowski S. , Socha-Hanc J. , Paszkowski A.
• Języki publikacji: EN

Abstrakty

EN

Alanine aminotransferase (AlaAT, EC 2.6.1.2) and glycine aminotransferase (GlyAT, EC 2.6.1.4), two different enzymes catalyzing transamination reactions with L-alanine as the amino-acid substrate, were examined in maize in which alanine participates substantially in nitrogen transport. Preparative PAGE of a partially purified preparation of aminotransferases from maize leaves gave 6 fractions differing in electrophoretic mobility. The fastest migrating fraction I represents AlaAT specific for L-alanine as amino donor and 2-oxoglutarate as amino acceptor. The remaining fractions showed three aminotransferase activities: L-alanine-2-oxoglutarate, L-alanine-glyoxylate and L-glutamate-glyoxylate. By means of molecular sieving on Zorbax SE-250 two groups of enzymes were distinguished in the PAGE fractions: of about 100 kDa and 50 kDa. Molecular mass of 104 kDa was ascribed to AlaAT in fraction I, while the molecular mass of the three enzymatic activities in 3 fractions of the low electrophoretic mobility was about 50 kDa. The response of these fractions to: aminooxyacetate, 3-chloro-L-alanine and competing amino acids promted us to suggest that five out of the six preparative PAGE fractions represented GlyAT isoforms, differing from each other by the L-glutamate-glyoxylate:L-alanine-glyoxylate:L-alanine-2-oxoglutarate activity ratio.

Słowa kluczowe

EN

alanine aminotransferase; enzyme; isoform; glycine aminotransferase; leaf; maize

• Wydawca: -
• Czasopismo: Acta Biochimica Polonica
• Rocznik: 1999
• Tom: 46
• Numer: 2
• Opis fizyczny: p.447-457,fig.

Twórcy

autor

Orzechowski S.

• Warsaw Agricultural University, Rakowiecka 26-30, 02-528 Warsaw, Poland

autor

Socha-Hanc J.

autor

Paszkowski A.

Bibliografia

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