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
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Research Support, Non-U.S. Gov't
MeSH terms
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Animals
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Carrier Proteins / chemistry*
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Cysteine / chemistry
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Disulfides
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Electrophoresis, Polyacrylamide Gel
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Insect Proteins*
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Moths
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Protein Binding
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Sulfhydryl Compounds / chemistry
Substances
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Carrier Proteins
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Disulfides
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Insect Proteins
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Sulfhydryl Compounds
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juvenile hormone-binding protein, insect
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Cysteine