Novel method for evaluation of the oligomeric structure of membrane proteins.
Assessment of the quaternary structure of membrane proteins by PAGE has been problematic owing to their relatively poor solubility in non-dissociative detergents. Here we report that several membrane proteins can be readily solubilized in their native quaternary structure with the use of the detergent perfluoro-octanoic acid (PFO). Further, PFO can be used with PAGE, thereby providing a novel, accessible tool with which to assess the molecular mass of homo-multimeric protein complexes.
Ramjeesingh
M
M
Cell Biology Department, Research Institute, Hospital for Sick Children, 555 University Avenue, Toronto, Ontario, Canada M5G 1X8.
Huan
L J
LJ
Garami
E
E
Bear
C E
CE
D000818:Animals; D001457:Anion Exchange Protein 1, Erythrocyte / Q000737:chemistry / Q000302:isolation & purification; D051398:Aquaporin 1; D020346:Aquaporins / Q000737:chemistry / Q000302:isolation & purification; D001789:Blood Group Antigens; D015153:Blotting, Western; D002210:Caprylates; D002462:Cell Membrane / Q000737:chemistry; D003593:Cytoplasm / Q000737:chemistry; D003902:Detergents; D004591:Electrophoresis, Polyacrylamide Gel; D005466:Fluorocarbons; D006801:Humans; D008565:Membrane Proteins / Q000737:chemistry* / Q000302:isolation & purification; D008970:Molecular Weight; D015221:Potassium Channels / Q000737:chemistry / Q000302:isolation & purification; D024661:Potassium Channels, Inwardly Rectifying; D011487:Protein Conformation; D051381:Rats; D011963:Receptors, GABA-A / Q000737:chemistry / Q000302:isolation & purification; D012995:Solubility; D014982:Xenopus laevis
C496020:AQP1 protein, human; D001457:Anion Exchange Protein 1, Erythrocyte; C496022:Aqp1 protein, rat; D020346:Aquaporins; D001789:Blood Group Antigens; D002210:Caprylates; D003902:Detergents; D005466:Fluorocarbons; D008565:Membrane Proteins; D015221:Potassium Channels; D024661:Potassium Channels, Inwardly Rectifying; D011963:Receptors, GABA-A; D051398:Aquaporin 1; C023036:perfluorooctanoic acid