| Title: | "The B proteins secreted by the tubular accessory sex glands of the male mealworm beetle, Tenebrio molitor, have sequence similarity to moth pheromone-binding proteins" |
| Address: | "Department of Zoology, University of Vermont, Burlington 05405-0086, USA" |
| DOI: | 10.1016/0965-1748(94)00085-v |
| ISSN/ISBN: | 0965-1748 (Print) 0965-1748 (Linking) |
| Abstract: | "B proteins represent one of the four major protein groups secreted by the tubular accessory glands of adult, male mealworm beetles. They are acidic proteins with an apparent molecular mass of 18.8 kDa. In this paper we present the deduced amino-acid sequences of two, almost identical B proteins, termed B1 and B2. The mature proteins are 118 amino acids long. They contain 11 (B2) or 12 (B1) possible phosphorylation sites and are rich in glutamic acid (16%). Lectin binding experiments indicate the presence of asparagine linked carbohydrate. The secondary structure of the B proteins is predicted to be almost completely alpha-helical. The B proteins show significant sequence resemblance to a group of pheromone- and odorant-binding proteins in moths and Drosophila, suggesting a role as carrier proteins for lipids" |
| Keywords: | "Amino Acid Sequence Animals Base Sequence Blotting, Northern Carrier Proteins/*chemistry/isolation & purification/*metabolism DNA, Complementary Databases, Factual Drosophila melanogaster/metabolism Female Gonads/*metabolism Intercellular Signaling Peptid;" |
| Notes: | "MedlinePaesen, G C Happ, G M eng AI-15662/AI/NIAID NIH HHS/ Comparative Study Research Support, U.S. Gov't, P.H.S. England 1995/03/01 Insect Biochem Mol Biol. 1995 Mar; 25(3):401-8. doi: 10.1016/0965-1748(94)00085-v" |
