Back to Search
Start Over
Expression of Recombinant AccMRJP1 Protein from Royal Jelly of Chinese Honeybee in Pichia pastoris and Its Proliferation Activity in an Insect Cell Line
- Source :
- Journal of Agricultural and Food Chemistry. 58:9190-9197
- Publication Year :
- 2010
- Publisher :
- American Chemical Society (ACS), 2010.
-
Abstract
- Major royal jelly protein 1 (MRJP1) is the most abundant member of the major royal jelly protein (MRJP) family of honeybee. Mature MRJP1 cDNA of the Chinese honeybee (Apis cerana cerana MRJP1, or AccMRJP1) was expressed in Pichia pastoris. SDS-PAGE showed that recombinant AccMRJP1 was identical in molecular weight to the glycosylated AmMRJP1 from the Western honeybee (Apis mellifera). Western blots probed with anti-AccMRJP1 antibody demonstrated that recombinant AccMRJP1 and soluble protein of the Western honeybee RJ (AmSPRJ) contained immunoreactive MRJP1. The 57 kDa protein in AmSPRJ contained an N-terminal amino sequence of N-I-L-R-G-E, which is identical to that previously characterized in AmMRJP1. The molecular weight of recombinant AccMRJP1 was decreased from 57 to 48 kDa after deglycosylation, indicating that AccMRJP1 was glycosylated. The recombinant AccMRJP1 significantly stimulated Tn-5B-4 cell growth, similar to AmSPRJ and fetal bovine serum, and affected cell shape and adhesion to the substrate.
- Subjects :
- DNA, Complementary
Insecta
food.ingredient
Molecular Sequence Data
Polymerase Chain Reaction
Pichia
Cell Line
law.invention
Pichia pastoris
food
law
Complementary DNA
Gene expression
Royal jelly
Animals
Amino Acid Sequence
Peptide sequence
Cell Proliferation
DNA Primers
Glycoproteins
Base Sequence
biology
Fatty Acids
General Chemistry
Bees
biology.organism_classification
Molecular biology
Cell culture
Recombinant DNA
Insect Proteins
General Agricultural and Biological Sciences
Fetal bovine serum
Subjects
Details
- ISSN :
- 15205118 and 00218561
- Volume :
- 58
- Database :
- OpenAIRE
- Journal :
- Journal of Agricultural and Food Chemistry
- Accession number :
- edsair.doi.dedup.....057a508d4fa353d924cf268a22d3efb6