NDLI: Purification And Properties Of Uridine Hydrolase From Mung-bean (Phaseolus Radiatus) Seedlings

Content Provider	Indian Institute of Science (IISc)
Author	Achar, B. S. Vaidyanathan, C. S.
Copyright Year	1967
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 À. 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.
File Format	PDF
Journal	PeerReviewed
Language	English
Publisher	Elsevier Science
Publisher Date	1967-01-01
Access Restriction	Authorized
Subject Keyword	Biochemistry
Content Type	Text
Resource Type	Article

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