Isolation and structure analysis of bee venom mast cell degranulating peptide.
The venom of Apis mellifera was processed by gel permeation chromatography on Sephadex G-50 and by reversed-phase HPLC. The initial gel permeation step was carried out in the presence of phosphate ions (0.5 M). Ion pair reagents were required to resolve the strongly basic peptides, secapin, mast cell degranulating (MCD-) peptide and apamin, by reversed-phase (RP) HPLC. Using this relatively simple procedure it is possible to isolate these peptides essentially free of melittin (less than 1 in 10(7)) and phospholipase (less than 1 in 10(5] in high yield. The CD spectrum and secondary structure analysis are reported for MCD-peptide and on this basis a solution structure is proposed for this toxin.
D000818:Animals; D001514:Bee Venoms / Q000032:analysis*; D001516:Bees; D002850:Chromatography, Gel; D002851:Chromatography, High Pressure Liquid; D002942:Circular Dichroism; D010455:Peptides / Q000302:isolation & purification*; D010710:Phosphates; D011487:Protein Conformation
D001514:Bee Venoms; D010455:Peptides; D010710:Phosphates; C008331:mast cell degranulating peptide