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

Citation

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

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.

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Additional Metadata

Item Type:	Article
Divisions:	Faculty of Environmental Studies
Publisher:	Universiti Pertanian Malaysia
Keywords:	ATP-sulphurylase; Purification; Properties; Oryza sativa; Sulphur metabolism
Depositing User:	Nur Izyan Mohd Zaki
Date Deposited:	09 Nov 2009 08:09
Last Modified:	09 Mar 2015 05:00
URI:	http://psasir.upm.edu.my/id/eprint/2046
Statistic Details:	View Download Statistic

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