Acyl Carrier Protein Interacts With Melittin

Creator(s)

Mary L. Ernst-Fonberg, Quillen-Dishner College of Medicine
Sande G. Williams, Quillen-Dishner College of Medicine
Lesa M.S. Worsham, Quillen-Dishner College of Medicine

Document Type

Article

Publication Date

9-18-1990

Description

Acyl carrier protein (ACP) from Escherichia coli has been shown to form complexes with melittin, a cationic peptide from bee venom. ACP is a small (Mr 8847), acidic, Ca2+-binding protein, which possesses some characteristics resembling those of regulatory Ca2+-binding proteins including interaction with melittin. Complexing between melittin and ACP which occurred both in the presence and absence of Ca2+ was evident by chemical cross-linking the two peptides, fluorescence changes (including anisotropy measurements), and inhibition by melittin of the activity of a nonaggregated fatty acid synthetase from Euglena. Also, anti-Apis mellifera antibodies which contained antibodies against melittin specifically inhibited the same enzyme system activity relative to non-immune IgG.

Citation Information

Ernst-Fonberg, Mary L.; Williams, Sande G.; and Worsham, Lesa M.S.. 1990. Acyl Carrier Protein Interacts With Melittin. Biochimica et Biophysica Acta (BBA)/Lipids and Lipid Metabolism. Vol.1046(2). 111-119. https://doi.org/10.1016/0005-2760(90)90177-Y PMID: 2223852 ISSN: 0005-2760