| Literature DB >> 12044491 |
M F Rosa de Lima1, C A Sanchez Ferreira, D R Joaquim de Freitas, J G Valenzuela, A Masuda.
Abstract
A cDNA of glutathione S-transferase (GST) was isolated from a cDNA library of salivary glands of Boophilus microplus. The recombinant protein was purified by glutathione affinity chromatography and assayed upon the chromogenic substrate CDNB. The 864 bp cloned fragment was sequenced and showed an open reading frame coding for a protein of 220 amino acids. Expression of the GST gene was tested by RT-PCR in tick tissues and larvae mRNA. Comparison of the deduced amino acid sequence with GSTs from other species revealed that the enzyme is closely related to the mammalian class mu GSTs.Entities:
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Year: 2002 PMID： 12044491 DOI： 10.1016/s0965-1748(01)00157-6
Source DB: PubMed Journal: Insect Biochem Mol Biol ISSN： 0965-1748 Impact factor: 4.714