Free access
Issue
Apidologie
Volume 32, Number 1, January-February 2001
Page(s) 69 - 80
DOI http://dx.doi.org/10.1051/apido:2001112

References

  • Albert S., Klaudiny J., Simúth J. (1999) Molecular characterization of MRJP3, highly polymorphic protein of honeybee (Apis mellifera L.) royal jelly, Insect Biochem. Mol. Biol. 29, 247-254.
  • Albert S., Bhattacharya D., Klaudiny J., Schmitzová J., Simúth J. (1999) The family of major royal jelly proteins and its evolution, J. Mol. Evol. 49 290-297.
  • Alberts B., Bray D., Lewis J., Raff M., Roberts K., Watson J.D. (1994) Molecular biology of the cell, Third edition, Gerland Publishing, New York-London, pp. 125-128.
  • Chen l.C., Chen S.Y. (1995) Changes in protein components and storage stability of Royal jelly under various conditions, Food Chemistry 54, 195-200.
  • Crailsheim K. (1991) Interadult feeding of jelly in honeybee (Apis mellifera L.) colonies, J. Comp. Physiol. B 161, 55-66.
  • Eisenstein E., Schachman H.K. (1989) Determining the roles of subunits in protein function, in: Creighton T.E. (Ed.), Protein Function, IRL Press, Oxford University, pp. 136-175.
  • Franks F. (1993) Internal structure and organisation, in: Franks F. (Ed.), Protein Biotechnology, The Humana Press, Totowa, New Jersey, pp. 91-133.
  • Hanes J., Simúth J. (1992) Identification and partial characterization of major royal jelly protein of honeybee (Apis mellifera L.), J. Apic. Res. 31, 22-26.
  • Júdová J., Klaudiny J., Simúth J. (1998) Preparation of recombinant most abundant protein MRJP1 of royal jelly, Biologia, Bratislava 56, 777-784.
  • Kimura Y., Washino N., Yonekura M. (1995) N-linked sugar chains of 350 kDa royal jelly glycoprotein, Biosci. Biotech. Biochem. 59, 507-509.
  • Klaudiny J., Kulifajová J., Crailsheim K., Simúth J. (1994a) New approach to the study of division of labour in honeybee colony (Apis mellifera L.), Apidologie 25, 596-600.
  • Klaudiny J., Hanes J., Kulifajová J., Albert S., Simúth J. (1994b) Molecular cloning of two cDNAs from the head of the nurse honeybee (Apis mellifera L.), J. Apic. Res. 33, 105-111.
  • Knecht D., Kaatz H.H. (1990) Patterns of larval food production by hypopharyngeal glands in adult worker honey bees, Apidologie 21, 457-468.
  • Kornezos A., Chia W. (1992) Apical secretion and association of the Drosophila yellow gene product with developing larval cuticle structures during embryogenesis, Mol. Gen. Genet. 235, 397-405.
  • Koseki T., Kitabatake N., Doi E. (1990) Freezing denaturation of ovalbumin at acidic pH, J. Biochem. 107, 389-394.
  • Kubo T., Sasaki M., Nakamura J., Sasagawa H., Ohashi K., Takuchi H. (1996) Change in the expression of hypopharyngeal-glands proteins of the worker honeybees (Apis mellifera L.) with the age and/or role, J. Biochem. 119, 291-295.
  • Kucharski R., Malezska R., Hayward D.C., Ball E.E. (1998) A royal jelly protein is expressed in a subset of Kenyon cells in the mushroom bodies of the honeybee brain, Naturwissenschaften 85, 343-346.
  • Laemmli U.K. (1970) Cleavage of structural proteins during the assembly of the head of bacteriophage T4, Nature 227, 680-685.
  • Lensky Y., Rakover Y. (1983) Separate protein body compartments of the worker honeybee (Apis mellifera L.), Comp. Biochem. Physiol. 75, 607-615.
  • Lercker G., Caboni M.F., Vecchi M.A., Sabatini A.G., Nanetti A. (1992) Caracterizzazione dei principali constituenti della gelatina reale, Apicoltura 8, 27-93.
  • Maleszka R., Kucharski R. (2000) Analysis of Drosophila yellow-B cDNA reveals a new family of proteins related to the royal jelly proteins in honeybee and to an orphan protein in unusal bacterium Deinococcus radiodurans, Biochem. Biophys. Res. Com. 27, 773-776.
  • Moritz R.F.A., Southwick E.E. (1992) Bees a superorganisms. An evolutionary reality, Springer- Verlag, Berlin, Heidelberg.
  • Ohashi K., Natori S., Kubo T. (1997) Change in the mode of gene expression of the hypopharyngeal gland cells with age-dependent role change of the honeybee Apis mellifera L., Eur. J. Biochem. 249, 797-802.
  • Rost B., Sander C. (1993) Prediction of protein secondary structure at better than 70% accuracy, J. Mol. Biol. 232, 584-599.
  • Sasaki M., Tsurtua T., Asada S. (1987) Roles of the physical property of royal jelly in queen differentiation of honeybees, in: Eder J., Rembold H. (Eds.), Chemistry and Biology of Social Insects, J., Peperny, München, pp. 306-307.
  • Schmidt J.O., Buchmann S.L. (1992) Other products of the hive, in: Graham J.M. (Ed.), The hive and the honey bee, Dadant and Sons, Hamilton, Illinois, pp. 968-969.
  • Schmitzová J., Klaudiny J., Albert S., Hanes J., Schroder W., Schrockengost V., Júdová J., Simúth J. (1998) A family of major royal jelly proteins of the honeybee Apis mellifera L., CMLS Cell Mol. Life Sci. 54, 1020-1030.
  • Stein P.E., Leslie A.G.W., Finch J.T., Carrell R.W. (1991) Crystal structure of uncleaved ovalbumin at 1.9 Åresolution, J. Mol. Biol. 221, 941-959.
  • Takenaka T. (1982) Chemical composition of royal jelly, Honeybee Sci. 3, 69-74 (in Japanese).
  • Tatsumi E., Hirose M. (1997) Highly ordered molten globule-like state of ovalbumin at acidic pH: native-like fragmentation by protease and selective modification of Cys367 with dithiodipyridine, J. Biochem. 122, 300-308.
  • Tsao W., Shuel R.W. (1968) Breakdown of royal jelly protein in the midgut of the larval honeybee, J. Apic. Res. 7, 119-128.


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