[Binding of phosphatidylinositol-3,4,5-triphosphate to 45-kDa sec14-like protein from the rat olfactory epithelium in liposomes].
The binding of phosphatidylinositol-3,4,5-triphosphate to a protein with molecular mass of 45 kDa from rat olfactory epithelium (p45) was investigated using a model membrane system. Liposomes containing a mixture of phospholipids (phosphatidylethanolamine, phosphatidylcholine, and phosphatidylinositol-3,4,5-triphosphate) were used in the study. The binding of the protein to liposomes caused by its interaction with phosphatidylinositol-3,4,5-triphosphate was confirmed by cosedimentation and immunoblotting with chemiluminescent detection using monoclonal antibodies to the native protein p45. The English version of the paper: Russian Journal of Bioorganic Chemistry, 2006, vol. 32, no. 3; see also http://www.maik.ru.
Il'nitskaia
E V
EV
Shamborant
O G
OG
Radchenko
V V
VV
Shuvaeva
T M
TM
Lipkin
V M
VM
D000818:Animals; D002352:Carrier Proteins / Q000737:chemistry* / Q000378:metabolism; D004848:Epithelium / Q000737:chemistry / Q000378:metabolism; D008081:Liposomes / Q000737:chemistry* / Q000378:metabolism; D009831:Olfactory Mucosa / Q000737:chemistry* / Q000378:metabolism; D018129:Phosphatidylinositol Phosphates / Q000737:chemistry* / Q000378:metabolism; D011485:Protein Binding / Q000502:physiology; D051381:Rats
D002352:Carrier Proteins; D008081:Liposomes; D018129:Phosphatidylinositol Phosphates