| Literature DB >> 15484261 |
Kalyani V P Guntur1, Daniel Velasquez, Linda Chadwell, Christopher Carroll, Susan Weintraub, J Aaron Cassill, Robert Renthal.
Abstract
Antennal proteins of the male fire ant (Solenopsis invicta) were analyzed by two-dimensional gel electrophoresis, with the objective of identifying pheromone-binding proteins, which have not previously been found in ant antennae. The major low-molecular weight protein found in the male fire ant antenna was subjected to Edman degradation to determine the N-terminal amino acid sequence. Degenerate PCR primers based on this sequence were used to obtain a cDNA sequence corresponding to the full-length protein sequence. In-gel trypsin digestion followed by MALDI-TOF mass spectrometry and HPLC-ESI/MS/MS demonstrated that the protein gel spot contained only the protein corresponding to the cDNA sequence obtained by PCR. The sequence is similar to apolipophorin-III, an exchangeable lipid-binding protein. Fire ant apolipophorin-III is expressed in the antenna as well as the head, thorax and abdomen. (c) 2004 Wiley-Liss, Inc.Entities:
Mesh:
Substances:
Year: 2004 PMID: 15484261 DOI: 10.1002/arch.20019
Source DB: PubMed Journal: Arch Insect Biochem Physiol ISSN: 0739-4462 Impact factor: 1.698