Free Access
Issue
Apidologie
Volume 31, Number 6, November/December 2000
Page(s) 671 - 677
DOI https://doi.org/10.1051/apido:2000151

References

1
Arbuthnot P.B., Cantill R.C., Herbum H.R., An electrophoretic characterization of African worker honey bee hemolymph proteins during development, Comp. Biochem. Physiol. B 74 (1983) 467-471.
2
Danty E., Arnold G., Burmester T., Huet J.C., Huet D., Pernollet J.C., Masson C., Identification and developmental profiles of hexamerins in antenna and hemolymph of the honeybee, Apis mellifera, Insect Biochem. Mol. Biol. 28 (1998) 387-397.
3
Engels W., Fahrenhorst H., Age-dependent and caste-dependent changes in hemolymph protein patterns of Apis mellifera, Wilhelm Roux Arch. Entwickl. mech. Org. 174 (1974) 285-296.
4
Glinski Z., Jarosz J., Polyacrylamide gel electrophoresis in observations on insect haemo-lymph, Med. Wet. 3 (1986) 159-164 (in Polish).
5
Glinski Z., Jarosz J., Werniski A., An immunoelectrophoretical analysis of soluble blood proteins of coiled and upright larvae of the worker honey bee, Apis mellifera, Apidologie 16 (1985) 247-265.
6
Huang Z.Y., Otis G.W., Teal P.E.A., Nature of brood signal activating the protein synthesis of hypopharyngeal gland in honey bees, Apis mellifera (Apidae, Hymenoptera), Apidologie 20 (1989) 455-464.
7
Ivanova E., Izsledvanija varchu elektroforeticnite spektri na raztvorimi beltaci pri Apis mellifera L., Plovdiv University, Trav. Sci. 29 (1991) 247-250.
8
Krieg P., Marek M., Protein and esterase changes in the hemolymph of the queens of honey bee, Apis mellifera L., Comp. Biochem. Physiol. B-Biochem. and Mol. Biol. 75 (1983) 513-517.
9
Kubo T., Sasaki M., Nakamura J., Sasagawa H., Ohashi K., Takeushi H., Natori S., Change in the expression of hypopharyngeal gland proteins of the worker honeybees (Apis mellifera L.) with age and/or role, J. Biochem. 119 (1996) 291-295.
10
Maurer G., Disk-elektroforez, Mir, Moskva, 1971.
11
Michelette E., Engels W., Concentration of hemolymph proteins during postembryonic worker development of Africanized honey bees in Brazil and Carniolans in Europe, Apidologie 26 (1995) 101-108.
12
Ohashi K., Natori S., Kubo T., 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 (1997) 797-802.
13
Ohashi K., Sawata M., Takeuchi H., Natori S., Kubo T., Molecular cloning of cDNA and analysis of expression of the gene far alpha-glucosidase from the hypopharyngeal gland of the honeybee Apis mellifera L., Biochem. Biophys. Res. Commun. 221 (1996) 380-385.
14
Popov P., Ivanova E., Electrophoretic studies on the total soluble protein in imago forms of Apis mellifera L., Animalia 30 (1994) 53-56.
15
Raolison C., Sutter B., An intestinal insulin-like molecule in Apis mellifera, Comp. Biochem. Physiol. A 69 (1981) 79-83.
16
Shao-Wen Li, Jang Qwen Mei, Meng Jo-Pin, Chang I., Studies on the haemolymph protein pattern of two species of honey bees Apis mellifera, Acta Entomol. Sin. 25 (1982) 185-190 (in Chinese).


Abstract

Copyright INRA/DIB/AGIB/EDP Sciences