Ammonia assimilation in <i>Vitis vinifera</i> L.: <p>III. Glutamate oxaloacetate transaminase from leaf and root tissue</p>

Authors

  • Kalliopi A. Roubelakis-Angelakis
  • W. M. Kliewer

DOI:

https://doi.org/10.5073/vitis.1984.23.37-41

Abstract

Glutamate-oxaloacetate transaminase (GOT) activities in Vitis vinifera L. cv. Chenin blanc leaf and root tissues were associated only with the soluble fraction. Mean in vitro enzyme activity of both tissues was 4.3 ± 0.8 μmol oxaloacetate formed per g fresh tissue per hour. Km values of GOT from leaves and roots were (1.9 ± 0.4) · 10-4 M for α-ketoglutarate and (4.7 ± 0.5) · 10-3 M for L-aspartate. Optimum in vitro conditions for GOT activity were pH 7.4-7.8, amount of enzyme equivalent to 95-130 mg fresh tissue and incubation temperature 38-39 °C. Neither leaf nor root GOT responded to exogenous pyridoxal-5' phosphate.

Die Ammonium-Assimilation bei Vitis vinifera L.:
III. GlutamatcOxalacetat-Transaminase aus Blatt- und Wurzelgewebe

Die Aktivität der Glutamat-Oxalacetat-Transaminase (GOT) in Blatt- und Wurzelgewebe der Rebsorte Chenin blanc (Vitis vinifera L.) war auf die lösliche Fraktion beschränkt. In vitro betrug die mittlere Enzymaktivität in beiden Organen 4,3 ± 0,8 μmol Oxalacetat je g Frischgewicht und h. Die Km-Werte von GOT aus Blättern und Wurzeln betrugen (1,9±0,4) . 10-4 M für α-Ketoglutarat und (4,7±0,5) · 10-3 M für L-Aspartat. Die optimalen Bedingungen der GOT-Aktivität waren in vitro ein pH von 7,4-7,8, eine Enzymmenge, die dem Gehalt von 95-130 mg Frischmaterial entsprach, und eine Inkubationstemperatur von 38-39 °C. Weder Blatt- noch Wurzel-GOT reagierten auf zugesetztes Pyridoxal-5'-Phosphat.

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Published

2016-02-08

Issue

Vol. 23 No. 1 (1984): Vitis

Section

Article

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