Cloning and partial characterization of a Boophilus microplus (Acari: Ixodidae) glutathione S-transferase.
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.
Rosa de Lima
M F
MF
Centro de Biotecnologia do Estado do Rio Grande do Sul, Universidade Federal do Rio Grande do Sul, C.P. 15005, Campus do Vale, 91501-970, Porto Alegre, RS, Brazil.
Sanchez Ferreira
C A
CA
Joaquim de Freitas
D R
DR
Valenzuela
J G
JG
Masuda
A
A
D000595:Amino Acid Sequence; D001483:Base Sequence; D015153:Blotting, Western / Q000379:methods; D003001:Cloning, Molecular; D018076:DNA, Complementary; D005982:Glutathione Transferase / Q000235:genetics* / Q000378:metabolism; D026863:Ixodidae / Q000201:enzymology*; D008969:Molecular Sequence Data; D020133:Reverse Transcriptase Polymerase Chain Reaction; D017422:Sequence Analysis, DNA; D017386:Sequence Homology, Amino Acid
D018076:DNA, Complementary; D005982:Glutathione Transferase