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Adenosine 5'-triphosphate sulphurylase from rice shoots: partial purification and properties

Mohamad, Aminuddin and Kooi, E. T. (1980) Adenosine 5'-triphosphate sulphurylase from rice shoots: partial purification and properties. Pertanika, 3 (1). pp. 32-39. ISSN 0126-6128

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Abstract

ATP-sulphurplase was found in the soluble fraction of cell extracts ofrice shoots. The enzyme was purified 44-fold by ammonium sulphate fractionation, DEAE-cellulose and sephadex G-200 chrmatography. The optimum temperature ofthe enzyme is around 40°C while its pH optimum is between 7.5-8.5. Mg++ is required for its activity but group VI anions (molybdate, sulphate, selenate, tungstate), EDTA, HgH, azide, cyanide, sulphide and fluoride are inhibitory. The Km values for APS and pyrophosphate are 4.5 pM and 9.0 pM respectively.

Item Type:Article
Keyword:ATP-sulphurylase; Purification; Properties; Oryza sativa; Sulphur metabolism
Faculty or Institute:Faculty of Environmental Studies
Publisher:Universiti Pertanian Malaysia
ID Code:2046
Deposited By: Nur Izyan Mohd Zaki
Deposited On:09 Nov 2009 16:09
Last Modified:09 Mar 2015 13:00

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