Multiple small molecular weight GTP-binding proteins in bovine brain cytosol. Purification and characterization of a 24KDa protein

Biochem Biophys Res Commun. 1988 Sep 30;155(3):1284-92. doi: 10.1016/s0006-291x(88)81280-4.

Abstract

We have separated multiple small Mr GTP-binding proteins (G-proteins) from bovine brain crude membranes, purified a novel 24KDa G protein (smg p25A) to near homogeneity and characterized it. In this paper, we have studied these small Mr G proteins in the cytosol fraction of bovine brain. [35S]GTP gamma S-binding activity is detected in the cytosol fraction but this activity is one-sixth to one-eighth of that of the crude membrane fraction. When G proteins in the cytosol fraction are purified by successive chromatographies on DEAE-cellulose, Ultrogel AcA-44, hydroxyapatite and Mono Q HR5/5 columns, multiple small Mr G proteins are separated. One of these G proteins shows a Mr of about 24KDa. Its physical, immunological and kinetic properties are indistinguishable from smg p25A. These results indicate that there are also multiple small Mr G proteins in the cytosol fraction of bovine brain, and suggest that one of the cytosol G proteins is the soluble form of smg p25A.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Animals
  • Brain Chemistry*
  • Cattle
  • Chromatography, Ion Exchange
  • Electrophoresis, Polyacrylamide Gel
  • GTP-Binding Proteins / analysis*
  • Molecular Weight

Substances

  • GTP-Binding Proteins