Two disulphide bridges are present in juvenile hormone binding protein from Galleria mellonella.
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.
Kołodziejczyk
R
R
Division of Biochemistry, Institute of Organic Chemistry, Biochemistry and Biotechnology, Wrocław University of Technology, Poland.
Dobryszycki
P
P
Ozyhar
A
A
Kochman
M
M
D000818:Animals; D002352:Carrier Proteins / Q000737:chemistry*; D003545:Cysteine / Q000737:chemistry; D004220:Disulfides; D004591:Electrophoresis, Polyacrylamide Gel; D019476:Insect Proteins; D009036:Moths; D011485:Protein Binding; D013438:Sulfhydryl Compounds / Q000737:chemistry
D002352:Carrier Proteins; D004220:Disulfides; D019476:Insect Proteins; D013438:Sulfhydryl Compounds; C035606:juvenile hormone-binding protein, insect; D003545:Cysteine