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References

  • 1
    Lindauer, M. (1952) Ein Beitrag zur Frage der Arbeitsteilung im bienenstaat. Z. Vergl. Physiol. 34, 299345.
  • 2
    Robinson, G.E. (1987) Hormonal regulation of age polyethism in the honeybee, Apis mellifera. In Neurobiology and Behavior of Honeybees (Menzel, R. & Mercer, R., eds), pp. 266279, Springer-Verlag, Berlin.
  • 3
    Sakagami, S. (1953) Untersuchungen uber die Arbeitsteilung in einen Zwergvolk der Honigbienen. Beitrage zur Biologie des Bienenvolkes, Apis mellifera L., I. Jap. J. Zool. 11, 117185.
  • 4
    Sasagawa, H., Sasaki, M. & Okada, I. (1989) Hormonal control of the division of labor in adult honeybees (Apis mellifera L.) I. Effect of methoprene on corpora allata and hypopharyngeal gland, and its a-glycosidase activity. Appl. Ent. Zool. 24 (1), 6677.
  • 5
    Winston, M.L. (1987) The Biology of the Honey Bee. Harvard University Press, Cambridge, MA, USA.
  • 6
    Rösch, G.A. (1930) Untersuchungen uber die Arbeitsteilung im Bienenstaat. 2. Teil: Die Tatigkeiten der Arbeitsbienen unter experimentell veranderten Bedingungen. Z. Vergl. Physiol. 12, 171.
  • 7
    Halberstadt, K. (1980) Elektrophoretische Untersuchungen zur Sekretionstätigkeit der Hypopharynxdrüse der Honigbiene (Apis mellifera). Insectes Sociaux, Paris 27, 6177.
  • 8
    Knecht, D. & Kaatz, H.H. (1990) Patterns of larval food production by hypopharyngeal glands in adult worker honey bees. Apidologie 21, 457468.
  • 9
    Simpson, J., Riedel, I.B.M. & Wilding, M. (1968) Invertase in the hypopharyngeal glands of the honeybee. J. Apic. Res. 7, 2936.
  • 10
    Kubo, T., Sasaki, M., Nakamura, J., Sasagawa, H., Ohashi, K., Takeuchi, H. & Natori, S. (1996) Change in the expression of hypopharyngeal-gland proteins of the worker honeybees (Apis mellifera L.) with age and/or role. J. Biochem. 119, 291295.
  • 11
    Ohashi, K., Natori, S. & Kubo, T. (1997) Change in the mode of gene expression of the hypopharyngeal gland cells with an age-dependent role change of the worker honeybee Apis mellifera L. Eur. J. Biochem. 249, 797802.
  • 12
    Klaudiny, J., Hanes, J., Kulifajova, J., Albert, S. & Simuth, J. (1994) Molecular cloning of two cDNAs from the head of the nurse honey bee (Apis mellifera L.) for coding related proteins of royal jelly. J. Apic. Res. 33 (2), 105111.
  • 13
    Albert, S., Klaudiny, J. & Simuth, J. (1996) Newly discovered features of the updated sequence of royal jelly protein RJP571; longer repetitive region on C-terminus and homology to Drosophila melanogaster yellow protein. J. Apic. Res. 35 (2), 6368.
  • 14
    Ohashi, K., Sawata, M., Takeuchi, H., Natori, S. & Kubo, T. (1996) Molecular cloning of cDNA and analysis of expression of the gene for α-glucosidase from the hypopharyngeal gland of the honeybee Apis mellifera L. Biochem. Biophys. Res. Commun. 221, 380385.
  • 15
    Diatchenko, L., Lau, Y.F., Campbell, A.P., Chenchik, A., Moqadam, F., Huang, B., Lukyanov, S., Lukyanov, K., Gurskaya, N., Sverdlov, E.D. & Siebert, P.D. (1996) Suppression subtractive hybridization: a method for generating differentially regulated or tissue-specific cDNA probes and libraries. Proc. Natl Acad. Sci. USA 93, 60256030.
  • 16
    Haq, S., Kubo, T., Kurata, S., Kobayashi, A. & Natori, S. (1996) Purification, characterization, and cDNA cloning of a galactose-specific C-type lectin from Drosophila melanogaster. J. Biol. Chem. 271, 2021320218.
  • 17
    Short, J.M., Fernandez, J.M., Sorge, J.A. & Huse, W.D. (1988) Lambda ZAPI: a bacteriophage lambda expression vector with in vivo excision properties. Nucleic Acids Res. 16, 75837600.
  • 18
    Henikoff, S. (1987) Unidirectional digestion with exonuclease III in DNA sequence analysis. Methods Enzymol. 155, 156165.
  • 19
    Sanger, F., Nicklen, S. & Coulson, A.R. (1977) DNA. sequencing with chain-terminating inhibitors. Proc. Natl Acad. Sci. USA 74, 54635467.
  • 20
    White, J.W. Jr, Subers, M.H. & Schepartz, A.I. (1963) The identification of inhibine, antibacterial factor in honey, as hydrogen peroxide, and its origin in a honey glucose oxidase system. Biochem. Biophys. Acta 73, 5770.
  • 21
    Bernfeld, P. (1955) Amylases, α and β. In Methods in Enzymology (Colowick, S.P. & Kaplan, N.O., eds), Vol. 1. pp. 149158.Academic Press, New York, USA.
  • 22
    Laemmli, U.K. (1970) Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 227, 680685.
  • 23
    Boer, P.H. & Hickey, D.a. (1986) The alpha-amylase gene in Drosophila melanogaster: nucleotide sequence, gene structure and expression motifs. Nucleic Acids Res. 14, 83998411.
  • 24
    Krasney, P.A., Carr, C. & Cavener, D.R. (1990) Evolution of the glucose dehydrogenase gene in Drosophila. Mol. Biol. Evol. 7, 155177.
  • 25
    Frederick, K.R., Tung, J., Emerick, R.S., Masiarz, F.R., Chamberlain, S.H., Vasavada, A., Rosenberg, S., Chakraborty, S., Schopter, L.M. & Massey, V. (1990) Glucose oxidase from Aspergillus niger. Cloning, gene sequence, secretion from Saccharomyces cerevisiae and kinetic analysis of a yeast-derived enzyme. J. Biol. Chem. 265, 37933802.
  • 26
    Pazur, J.H., Kleppe, K. & Ball, E.M. (1963) The glycoprotein nature of some fungal carbohydrates. Arch. Biochem. Biophys. 103, 515516.