Free access
Issue
Apidologie
Volume 35, Number 4, July-August 2004
Page(s) 371 - 381
DOI http://dx.doi.org/10.1051/apido:2004029
Apidologie 35 (2004) 371-381
DOI: 10.1051/apido:2004029

Proteins in spermathecal gland secretion and spermathecal fluid and the properties of a 29 kDa protein in queens of Apis mellifera

Michael Klenka, Gudrun Koenigera, Nikolaus Koenigera and Hugo Fasoldb

a  Institut für Bienenkunde (Polytechnische Gesellschaft), FB Biologie der J.W. Goethe-Universität Frankfurt, Karl-von-Frisch-Weg 2, 61440 Oberursel, Germany
b  Institut für Biochemie der J.W. Goethe-Universität Frankfurt, Marie-Curie-Str. 9-11, 60053Frankfurt, Germany

(Received 24 April 2003; revised 30 July 2003; accepted 29 September 2003)

Abstract - One and two dimensional SDS-PAGE were used to characterize the protein pattern of the spermathecal gland secretion and spermathecal fluid in Apis mellifera queen pupae and emerged queens of different ages. The concentration of protein varied from 8.5 and 15.3 mg/mL in the spermathecal fluid, and from 5 to 8.5 mg/mL in the secretion. Development of the protein pattern of the gland secretion and spermathecal fluid was identical from pupae until the age of 3 days. In sexually mature queens (10 days or older) the gland secretion and spermathecal fluid each had one additional band at 79 kDa and at 29 kDa respectively. The 29 kDa protein was N-terminal blocked but several peptide fragments were sequenced after digestion with LysC protease. Only 2 of the sequences showed a distinct homology to the N-terminal half of the glycolytic enzyme triosephosphate isomerase (TPI). TPI antibody reacted with the 29 kDa protein, but the enzymatic activity was only 1/100 compared to TPI of hemolymph. The possible function of the protein is discussed.


Key words: spermatheca / sperm storage / protein pattern / 29 kDa protein / Apis mellifera

Corresponding author: Gudrun Koeniger Bienenkunde@em.uni-frankfurt.de

© INRA, EDP Sciences, DIB, AGIB 2004