Apisimin, a new serine-valine-rich peptide from honeybee (Apis mellifera L.) royal jelly: purification and molecular characterization
Overview of Bíliková K et al.
| Authors | Bíliková K Hanes J Nordhoff E Saenger W Klaudiny J Simúth J |
|---|---|
| Affiliation | Laboratory of Genetic Engineering Institute of Chemistry Slovak Academy of Sciences Dúbravská cesta 9 SK-84238 Bratislava Slovak Republic. |
| Journal | FEBS Lett |
| Year | 2002 |
Abstract
A peptide named apisimin was found in honeybee (Apis mellifera L.) royal jelly (RJ). N-terminal sequencing showed that this peptide corresponded to the sequence of a cDNA clone isolated from an expression cDNA library prepared from heads of nurse honeybees. No homology was found between the protein sequence of apisimin with a molecular mass of 5540.4 Da and sequences deposited in the Swiss-Prot database. The 54 amino acids of apisimin do not include Cys, Met, Pro, Arg, His, Tyr, and Trp residues. The peptide shows a well-defined secondary structure as observed by CD spectroscopy, and has the tendency to form oligomers. Isoelectrofocusing showed apisimin to be an acidic peptide.