Purification and subunit composition of a GTP-binding protein from maize root plasma membranes.
When frozen plasma membranes isolated from maize seedling roots are thawed, a significant portion of GTP-binding activity goes into solution. The GTP-binding protein was purified by ion exchange chromatography on Mono-Q and gel filtration on Superose 6. Its molecular weight was estimated at 61 kDa by gel filtration. The same molecular weight was obtained upon solubilization of the GTP-binding protein with cholic acid followed by gel filtration in the presence of this detergent. SDS-PAGE demonstrated that the isolated GTP-binding protein consists of two types of subunit of molecular weights 27 kDa and 34 kDa.
Institute of Agricultural Biotechnology, Moscow, USSR.
S V
SV
Bilushi
A G
AG
Shebunin
A V
AV
Babakov
D002462:Cell Membrane / Q000737:chemistry; D002850:Chromatography, Gel; D004591:Electrophoresis, Polyacrylamide Gel; D019204:GTP-Binding Proteins / Q000737:chemistry / Q000302:isolation & purification*; D008565:Membrane Proteins / Q000737:chemistry / Q000302:isolation & purification*; D008970:Molecular Weight; D010940:Plant Proteins / Q000737:chemistry / Q000302:isolation & purification*; D003313:Zea mays / Q000737:chemistry*
D008565:Membrane Proteins; D010940:Plant Proteins; D019204:GTP-Binding Proteins