Interaction of glucagon with dimyristoyl glycerophosphocholine

摘要: Abstract Glucagon can form amphipathic helices and interact with dimyristoyl glycerophosphocholine at temperatures below the phase transition leading to a shift in fluorescence emission maximum of tryptophan from 350 338 nm 3-fold enhancement intensity as well change polarization fluorescence. The circular dichroism properties lipid-associated glucagon indicates that it has an increased content α-helix. temperature lipid monitored by pyrene excimer is not altered interaction although higher glucagon/lipid ratios decrease formation noted low temperature. Above temperature, addition no effect on or glucagon. Thus this hormone stronger than above it.