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  • Title: Uridine phosphorylase from Escherichia coli B. Enzymatic and molecular properties.
    Author: Vita A, Amici A, Cacciamani T, Lanciotti M, Magni G.
    Journal: Int J Biochem; 1986; 18(5):431-5. PubMed ID: 3519310.
    Abstract:
    Uridine phosphorylase (EC 2.4.2.3) from Escherichia coli B is an oligomeric protein composed of four identical subunits of 29,000 mol. wt. The enzyme has four half-cystine residues per subunit titrable only in denaturing condition. No disulphide linkages either inter- or intra-chain are present. The isoelectric point is 5.25. The enzyme shows strict specificity toward uridine and 5-methyluridine and is inhibited by thymine, deoxycytidine and heavy metal ions.
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