Literature DB >> 122568

Purine nucleoside phosphorylase from bovine liver.

Z Ikezawa1, T Nishino, K Murakami, K Tsushima.   

Abstract

1. Purine nucleoside phosphorylase (purine nucleoside:orthophosphate ribosyltransferase, E.C. 2.4.2.1) from liver of cattle, Bos taurus, was purified to homogeneity. Some properties of the enzymes from three different bovine tissues were compared and discussed. 2. The enzyme has a molecular weight of 83,000, a sedimentation coefficient of 5.3 S, a Stokes' radius of 3.71 nm, a frictional ratio of 1.30 and a subunit molecular weight of 30,000. 3. Optimal pH for xanthosine degradation is around 5.5, whereas a broad pH activity profile for inosine degradation was observed between 5.0 and 7.5. Lineweaver-Burk plots curved downward at high concentrations of substrates, inosine, phosphate and arsenate.

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Year:  1978        PMID: 122568     DOI: 10.1016/0305-0491(78)90113-x

Source DB:  PubMed          Journal:  Comp Biochem Physiol B        ISSN: 0305-0491


  2 in total

1.  Isolation and characterization of mutations in the Escherichia coli regulatory protein XapR.

Authors:  C Jørgensen; G Dandanell
Journal:  J Bacteriol       Date:  1999-07       Impact factor: 3.490

2.  Identification and characterization of genes (xapA, xapB, and xapR) involved in xanthosine catabolism in Escherichia coli.

Authors:  C Seeger; C Poulsen; G Dandanell
Journal:  J Bacteriol       Date:  1995-10       Impact factor: 3.490

  2 in total

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