Two disulphide bridges are present in juvenile hormone binding protein from Galleria mellonella

Acta Biochim Pol. 2001;48(4):917-20.

Abstract

The hemolymph juvenile hormone binding protein (JHBP) from Galleria mellonella contains two disulphide bridges/molecule and no free Cys residues. An alignment of primary structures of other Lepidopteran JHBPs indicates that Cys residues, equivalent to Cys10,17,151,195 in G. mellonella JHBP, maybe involved in -S-S- bridge formation.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Animals
  • Carrier Proteins / chemistry*
  • Cysteine / chemistry
  • Disulfides
  • Electrophoresis, Polyacrylamide Gel
  • Insect Proteins*
  • Moths
  • Protein Binding
  • Sulfhydryl Compounds / chemistry

Substances

  • Carrier Proteins
  • Disulfides
  • Insect Proteins
  • Sulfhydryl Compounds
  • juvenile hormone-binding protein, insect
  • Cysteine