期刊
ARCHIVES OF INSECT BIOCHEMISTRY AND PHYSIOLOGY
卷 57, 期 3, 页码 101-110出版社
WILEY
DOI: 10.1002/arch.20019
关键词
olfaction; pheromone-binding proteins; encapsulins; apolipophorin; mass spectrometry
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 moss 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. Arch. Insect Biochem. Physiol. 57:101-110, 2004. (C) 2004 Wiley-Liss, Inc.
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