| Title: | Heterogeneity of odorant-binding proteins in the antennae of Bombyx mori |
| Author(s): | Maida R; Proebstl T; Laue M; |
| Address: | "Max-Planck-Institut fur Verhaltensphysiologie, Seewiesen, Germany" |
| ISSN/ISBN: | 0379-864X (Print) 0379-864X (Linking) |
| Abstract: | "Different odorant-binding proteins (OBPs) were isolated from total antennal homogenates of male and female Bombyx mori. Proteins were separated according to their isoelectric point by using preparative fast-flow isoelectrofocusing. Odorant-binding proteins were identified in immunoblots by antisera raised against the pheromone-binding protein (anti-PBP) and the general odorant-binding protein (anti-GOBP2) of Antheraea polyphemus. Four proteins cross-reacting with anti-PBP were detected in males and two in females, while three proteins cross-reacting with anti-GOBP2 were found in males and five in females. Both anti-PBP and anti-GOBP2 cross-reacting proteins had an apparent molecular weight of 15-16 kDa. In parallel, the same two antisera were used in immunocytochemical studies in order to determine the distribution of these proteins within the various subtypes of olfactory sensilla. The presence of multiple odorant-binding proteins within one moth species as well as their complex distribution pattern support the suggestion that soluble OBPs might have a function in odorant discrimination" |
| Keywords: | "Animals Blotting, Western Bombyx/anatomy & histology/*metabolism Cross Reactions Female Immune Sera Insect Proteins/immunology Isoelectric Focusing Male Olfactory Pathways/*metabolism Receptors, Odorant/immunology/*metabolism;" |
| Notes: | "MedlineMaida, R Proebstl, T Laue, M eng England 1997/11/18 Chem Senses. 1997 Oct; 22(5):503-15. doi: 10.1093/chemse/22.5.503" |
