作者: Mary Lou Ernst-Fonberg , Sande G. Williams , Lesa M.S. Worsham
DOI: 10.1016/0005-2760(90)90177-Y
关键词: Biochemistry 、 Peptide 、 Melittin 、 Tris 、 Fluorescence spectrometry 、 Acyl carrier protein 、 Binding protein 、 Biology 、 Enzyme 、 Euglena gracilis
摘要: Acyl carrier protein (ACP) from Escherichia coli has been shown to form complexes with melittin, a cationic peptide bee venom. ACP is small (Mr 8847), acidic, Ca2+-binding protein, which possesses some characteristics resembling those of regulatory proteins including interaction melittin. Complexing between melittin and occurred both in the presence absence Ca2+ was evident by chemical cross-linking two peptides, fluorescence changes (including anisotropy measurements), inhibition activity nonaggregated fatty acid synthetase Euglena. Also, anti-Apis mellifera antibodies contained against specifically inhibited same enzyme system relative non-immune IgG.