Apisimin, a new serine–valine‐rich peptide from honeybee (Apis mellifera L.) royal jelly: purification and molecular characterization

FEBS Letters

Šimúth, J²  Bı́liková, K²  Klaudiny, J²  Nordhoff, E³  Hanes, J²  Saenger, W¹ 

[1]Institute of Chemistry/Crystallography, Free University Berlin, Takustrasse 6, D-14195 Berlin, Germany

[2]Laboratory of Genetic Engineering, Institute of Chemistry, Slovak Academy of Sciences, Dúbravská cesta 9, SK-84238 Bratislava, Slovak Republic

[3]Max-Planck Institute of Molecular Genetics, Ihnestrasse 73, D-14195 Berlin, Germany

关键词: Honeybee (Apis mellifera L.);    Royal jelly;    Apisimin;    Serine–valine-rich peptide;    Honeybee peptide;    CD;    circular dichroism;    FPLC;    fast flow protein liquid chromatography;    IEF;    isoelectrocusing;    MALDI-TOF;    matrix-assisted laser-desorption ionization time-of-flight;    MBP;    maltose-binding protein;    MBP–apisimin;    recombinant fusion of maltose-binding protein with apisimin;    MRJPs;    major royal jelly proteins;    MRJP1;    apalbumin;    pI;    isoelectric point;    RJ;    royal jelly;    Tricine–SDS–PAGE;    tricine sodium dodecyl sulfate polyacrylamide gel electrophoresis;   

DOI  :  10.1016/S0014-5793(02)03272-6

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

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.

【 授权许可】

Unknown