Purification and subunit composition of a GTP‐binding protein from maize root plasma membranes

FEBS Letters

Shebunin, Alexander G.¹  Babakov, Alexey V.¹  Bilushi, Sevo V.¹ 

[1] Institute of Agricultural Biotechnology, Moscow, 127253, USSR

关键词: Maize;    GTP-binding protein;    Isolation;    Subunit;   

DOI  :  10.1016/0014-5793(91)81288-J

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

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.

【 授权许可】

Unknown