Characterization of the basic major royal jelly protein MRJP2 of honeybee (Apis mellifera) and its preparation by heterologous expression in E-coli

Authors
Bilikova, K Klaudiny, J Simuth, J
Citation
K. Bilikova et al., Characterization of the basic major royal jelly protein MRJP2 of honeybee (Apis mellifera) and its preparation by heterologous expression in E-coli, BIOLOGIA, 54(6), 1999, pp. 733-739
Citations number
17
Categorie Soggetti
Biology
Journal title
BIOLOGIA
ISSN journal
00063088 → ACNP
Volume
54
Issue
6
Year of publication
1999
Pages
733 - 739
Database
ISI
SICI code
0006-3088(199912)54:6<733:COTBMR>2.0.ZU;2-C
Abstract
Major proteins of honeybee (Apis mellifera L.) royal jelly (RJ) are members of the MRJP protein family. The second most abundant protein of RJ is the protein named MRJP2. In this report we describe the isolation of MRJP2 by i on exchange column chromatography and its molecular characterization as wel l as the preparation of recombinant MRJP2 by heterologous expression in E. coli. The SDS-PAGE homogenous 49 kDa protein is composed of eight proteins with different isoelectric points in the range of 7.5 to 8.5 pH.