Towards royal jelly proteome
| Autor: | Anna Gloria Sabatini, Donatella Fortunato, Elena Donadio, Romano Felicioli, Antonio Felicioli, Maria Gabriella Giuffrida, Roberta Scarselli, Ettore Balestreri, Amedeo Conti, M Pinzauti |
|---|---|
| Rok vydání: | 2005 |
| Předmět: |
food.ingredient
Proteome medicine.medical_treatment Molecular Sequence Data Apalbumin Royal jelly Biology Biochemistry Genome food Botany medicine Animals De novo sequencing Electrophoresis Gel Two-Dimensional Amino Acid Sequence Molecular Biology Gel electrophoresis Protease Fatty Acids fungi digestive oral and skin physiology food and beverages Honey Protein composition Bees Spectrometry Mass Matrix-Assisted Laser Desorption-Ionization behavior and behavior mechanisms Insect Proteins Female Apis mellifera Pollen-bread |
| Zdroj: | Proteomics (Weinh., Print) 5 (2005): 769–776. doi:10.1002/pmic.200401149 info:cnr-pdr/source/autori:Scarselli R., Donadio E., Giuffrida M.G., Fortunato D., Conti A., Balestreri E., Felicioli R., Pinzauti M., Sabatini A.G., Felicioli A./titolo:Towards royal jelly proteome/doi:10.1002%2Fpmic.200401149/rivista:Proteomics (Weinh., Print)/anno:2005/pagina_da:769/pagina_a:776/intervallo_pagine:769–776/volume:5 |
| ISSN: | 1615-9853 |
| DOI: | 10.1002/pmic.200401149 |
| Popis: | The recent availability of the honey-bee Apis mellifera genome and trascriptome of both the female castes, has stimulated new efforts in investigating the protein composition of royal jelly (RJ), its role in caste differentiation and its quality and typicality by a proteomic approach. This study is aimed both to separate and identify proteins of royal jelly and to detect some of them in honey-bee pollen-bread by using two-dimensional gel electrophoresis, mass spectrometry and by de novo sequencing. All the identified proteins belonged to the Apis mellifera genome. Apalbumin 1 was also confirmed to be present in honey-bee pollen-bread where the presence of apalbumin 2 was also found. In addition several fragments of apalbumin 1 and apalbumin 3 were also found in RJ. These could be the result of protease activity other than that of serine-protease. This study is a contribution to the description of royal jelly proteome. |
| Databáze: | OpenAIRE |
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