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Adenosine-5’-Triphosphate Sulphurylase from Rice Shoots: Partial Purification and Properties

M. Aminuddin and E. T. Kooi

Pertanika Journal of Tropical Agricultural Science, Volume 3, Issue 1, July 1980

Keywords: ATP-sulphurylase, purification, properties, Oryza sativa, Sulphur metabolism.

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ATP-sulphurplase was found in the soluble fraction of cell extracts of rice shoots. The enzyme was purified 44-fold by ammonium sulphate fractionation, DEAE-cellulose and sephadex G-200 chrmatography. The optimum temperature of the 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, Hg2+, azide, cyanide, sulphide and fluoride are inhibitory. The Km values for APS and pyrophosphate are 4.5 µM and 9.0 µM respectively.

ISSN 1511-3701

e-ISSN 2231-8542

Article ID

PERT-0060-1980

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