Free Access
Issue
Apidologie
Volume 32, Number 3, May-June 2001
Page(s) 275 - 283
DOI https://doi.org/10.1051/apido:2001129

References

  • Bonvehí J.S., Jordá R.E. (1991) Studie über die mikrobiologische Qualität und bacteriostatische Aktivität des Weiselfuttersaftes (Gelée Royale): Beeinflussung durch organische Säuren, Deutsche Lebensmittel-Rundschau 87, 256-259.
  • Bradford M.M. (1976) A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding, Anal. Biochem. 72, 248-254.
  • Brødsgaard C.J., Ritter W., Hansen H. (1998) Response of in vitro reared honey bee larvae to various doses of Paenibacillus larvae larvae spores, Apidologie 29, 1-10.
  • Bulet P., Hetru C., Dimarcq J.-L., Hoffmann D. (1999) Antimicrobial peptides in insects; structure and function, Dev. Comp. Imunol. 23, 329-344.
  • Casteels P., Ampe Ch., Jacobs F., Vaeck M.,Tempst P. (1989) Apideacins: antibacterial peptides from honeybees, EMBO J. 8, 2387-2391.
  • Casteels P., Ampe Ch., Riviere L., Van Damme J., Elicone Ch., Fleming M., Jacobs F., Tempst P. (1990) Isolation and characterization of abaecin, a major antibacterial response peptide in the honeybee (Apis mellifera), Eur. J. Biochem. 187, 381-386.
  • Casteels P., Ampe Ch., Jacobs F., Tempst P. (1993) Functional and chemical characterization of Hymenoptaecin, an antibacterial polypeptide that is infection-inducible in the honeybee (Apis mellifera), J. Biol. Chem. 268, 7044-7054.
  • Chen I.C., Chen S.Y. (1995) Changes in protein components and storage stability of royal jelly under various conditions, Food Chem. 54, 195-200.
  • Fujiwara S., Imai J., Fujiwara M., Yaeshima T., Kawashima T., Kobayashi K. (1990) A potent antibacterial protein in royal jelly, J. Biol. Chem. 265, 11333-11337.
  • Glinski Z., Jarosz J. (1995) Cellular and humoral defences in honey bees, Bee world 76, 195-205.
  • Hanes J., Simúth J. (1992) Identification and partial characterization of the major royal jelly protein of the honey bee (Apis mellifera L.), J. Apic. Res. 31, 22-26.
  • Hansen H., Brodsgaard C.J. (1999) American foulbrood: a review of its biology, diagnosis and control, Bee World 80, 5-23.
  • Hornitzky M., Oldroyd B.P., Somerville D. (1996) Bacillus larvae carrier status of swarms and feral colonies of honeybees (Apis mellifera) in Australia, Aust. Vet. J. 73, 116-117.
  • Miyagi T., Peng Ch.Y.S., Chuang R.Y., Mussen E.C., Spivak M.S., Doi R.H. (2000) Verification of oxytetracycline-resistant American foulbrood pathogen Paenibacillus larvae in the United States, J. Invertebr. Pathol. 75, 95-96.
  • 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, 797-802.
  • Otvos L.J.R. (2000) Antibacterial peptides isolated from insects, J. Peptide Sci. 6, 497-511.
  • Schägger H., Von Jagow G. (1987) Tricine-sodium dodecyl sulfate-polyacrylamide gel electrophoresis for the separation of proteins in the range from 1 to 100 kDa, Anal. Biochem. 166, 368-379.
  • Smith P.K., Krohn R.I., Hermanson G.T., Mallia A.K., Gartner F.H., Provenzano M.D., Fujimoto E.K., Goeke N.M., Olson B.J., Klenk D.C. (1985) Measurement of protein using bicinchonioic acid, Anal. Biochem. 150, 76-85.
  • Schmitzová J., Klaudiny J., Albert S., Schröder W., Schrockengost W., Hanes J., Júdová J., Simúth J. (1998) A family of major royal jelly proteins of the honeybee Apis mellifera L., Cell. Mol. Life Sci. 54, 1020-1030.
  • Spivak M., Gilliam M. (1993) Facultative expression of hygienic behaviour of honey bees in relation to disease resistance, J. Apic. Res. 32, 147-157.
  • Simúth J. (2001) Some properties of the main protein of honeybee (Apis mellifera L.) royal jelly, Apidologie 32, 69-80.
  • Taber S. (1988) Honey bee genetics, Gleanings Bee Cult. 116, 68-69.
  • Terras F.R.G., Schoofs H.M.E., De Bolle M.F.C., Van Leuven F., Rees S.B., Vanderleyden J., Cammue B.P.A., Broekaert W.F. (1992) Analysis of two novel classes of plant antifungal proteins from radish (Raphanus sativus L.) seeds, J. Biol. Chem. 267, 15301-15309.


Abstract

Copyright INRA/DIB/AGIB/EDP Sciences