Characterization of incomplete vitellogenin (VgC) in the Indian freshwater murrel, Channa punctatus (Bloch)
A novel incomplete vitellogenin (VgC) was purified from the plasma of estradiol-treated male murrel, Channa punctatus, by gel filtration chromatography. The native mass of VgC protein was 180 kDa, and it resolved as a single peptide of 100 kDa on SDS-PAGE. The peptide on subjecting to matrix-assisted laser desorption/ionization-time of flight produced a peptide mass fingerprint. On tandem mass spectrometry, some of these peptides showed mass to charge (m/z) ratio and amino acid sequence similarity with VgC peptides of other teleosts. Phylogenetic analysis revealed a similarity of murrel VgC with fish species of the order Perciformes. Semi-quantitative RT-PCR assay was developed to study expression of vgc gene at variable levels of estradiol exposure. Presence of VgC in males indicates that fish has been exposed to estrogens; hence, it can be used as a biomarker for estrogenic exposure.
KeywordsIncomplete vitellogenin (VgC) MALDI-TOF–MS/MS Channa punctatus RT-PCR
This work was supported by Research Grant from the University of Delhi, Delhi. One of us (SP) is thankful to CSIR, New Delhi, for the award of a Senior Research Fellowship.
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