Literature DB >> 8387372

The nucleotidase of Boophilus microplus and its relationship to enzymes from the rat and Escherichia coli.

P Willadsen1, G A Riding, J Jarmey, A Atkins.   

Abstract

Boophilus microplus contains a nucleotidase-like enzyme which is able to hydrolyze a range of nucleoside 5'-mono-, di- and triphosphates to the nucleoside. Its relationship to several other nucleotide hydrolyzing enzymes has been explored. Limited peptide sequencing shows similarities to both mammalian nucleotidases and the Escherichia coli uridine diphosphate sugar hydrolase. The tick enzyme also hydrolyzes UDP-glucose, though by a mechanism different to that of the bacterial enzyme. On the other hand, it resembles the mammalian nucleotidases in that there is evidence that it is attached to the cell membrane by a glycosyl-phosphatidylinositol (GPI) anchor.

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Year:  1993        PMID: 8387372     DOI: 10.1016/0965-1748(93)90010-p

Source DB:  PubMed          Journal:  Insect Biochem Mol Biol        ISSN: 0965-1748            Impact factor:   4.714


  3 in total

1.  Localisation and functional studies on the 5'-nucleotidase of the cattle tick Boophilus microplus.

Authors:  N Liyou; S Hamilton; R Mckenna; C Elvin; P Willadsen
Journal:  Exp Appl Acarol       Date:  2000-03       Impact factor: 2.132

2.  The salivary gland-specific apyrase of the mosquito Aedes aegypti is a member of the 5'-nucleotidase family.

Authors:  D E Champagne; C T Smartt; J M Ribeiro; A A James
Journal:  Proc Natl Acad Sci U S A       Date:  1995-01-31       Impact factor: 11.205

3.  Experimental vaccination of sheep and cattle against tick infestation using recombinant 5'-nucleotidase.

Authors:  M Hope; X Jiang; J Gough; L Cadogan; P Josh; N Jonsson; P Willadsen
Journal:  Parasite Immunol       Date:  2010-02       Impact factor: 2.280

  3 in total

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