Latrotoxin-like properties of a protein from brain.
In bovine brain cortex cytoplasm we have identified a soluble protein (L-protein) of M(r) approximately 90 kDa interacting with polyclonal antibodies to alpha-latrotoxin. The L-protein forms potential-dependent and cation-selective ion channels in BLM, which are blocked by Cd2+. The fusogenic activity of the L-protein was demonstrated on liposomes. We have arrived at the conclusion that the action mechanisms of the L-protein and alpha-latrotoxin are similar.
Zhukareva
V A
VA
Palladin Institute of Biochemistry, Ukrainian Academy of Sciences, Kiev, USSR.
Shatursky OYa
Lishko
V K
VK
Malysheva
M K
MK
Terletskaya YaT
Tsygankova
O M
OM
Grishin
E V
EV
D000818:Animals; D002417:Cattle; D002540:Cerebral Cortex / Q000737:chemistry*; D008051:Lipid Bilayers / Q000737:chemistry; D008081:Liposomes / Q000737:chemistry; D008564:Membrane Potentials; D008970:Molecular Weight; D009419:Nerve Tissue Proteins / Q000737:chemistry* / Q000302:isolation & purification; D012995:Solubility; D013111:Spider Venoms / Q000737:chemistry*
D008051:Lipid Bilayers; D008081:Liposomes; D009419:Nerve Tissue Proteins; D013111:Spider Venoms; C020763:alpha-latrotoxin