Mohamad, Aminuddin and Kooi, E. T. (1980) Adenosine -5' -Triphosphate Sulphurylase from Rice Shoots: Partial Purification and Properties. Pertanika, 3 (1). pp. 32-39.
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.
|Keyword:||ATP-sulphurylase, purification, properties, Oryza sativa, sulphur metabolism|
|Faculty or Institute:||Faculty of Environmental Studies|
|Deposited By:||Nur Izyan Mohd Zaki|
|Deposited On:||09 Nov 2009 16:09|
|Last Modified:||27 Jul 2010 09:50|
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