Purification and properties of uridine hydrolase from mung-bean (Phaseolus radiatus) seedlings

Achar, BS and Vaidyanathan, CS (1967) Purification and properties of uridine hydrolase from mung-bean (Phaseolus radiatus) seedlings. In: Archives of Biochemistry and Biophysics, 119 . 356 -362.

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Abstract

The occurrence in plants of an enzyme system catalyzing the cleavage of uridine has been demonstrated. The enzyme from Phaseolus radiatus was purified about 132-fold with 24% recovery by a combination of procedures involving mild acid treatment, ammonium sulphate fractionation, negative adsorption on calcium phosphate gel and DEAE-cellulose chromatography. The enzyme cleaves uridine to uracil and ribose in the absence of phosphate indicating that the mechanism of cleavage was hydrolytic rather than phosphorolytic. The enzyme is specific to uridine and does not act on other purine and pyrimidine compounds. The enzyme shows maximum activity at pH 7.4 and has a temperature optimum of 45 °. It does not require metal ions for activity. Inhibition of the enzyme by p-chloromercuribenzoate as well as N-ethylmaleimide and the reversal of p-chloromercuribenzoate inhibition by sulfhydryl agents indicate the probable involvement of readily oxidizable sulfhydryl groups in enzyme activity.

Item Type:	Journal Article
Publication:	Archives of Biochemistry and Biophysics
Publisher:	Elsevier Science
Additional Information:	Copy right of this article belongs to Elsevier Science.
Department/Centre:	Division of Biological Sciences > Biochemistry
Date Deposited:	13 May 2010 06:20
Last Modified:	23 Feb 2012 06:34
URI:	http://eprints.iisc.ac.in/id/eprint/27776

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