Biochemical characterization of Artemia ras p21

A Gandarillas; J Renart; M Quintanilla

doi:10.1007/BF00229640

Biochemical characterization of Artemia ras p21

Mol Cell Biochem. 1992 May 13;112(1):29-33. doi: 10.1007/BF00229640.

Authors

A Gandarillas¹, J Renart, M Quintanilla

Affiliation

¹ Instituto de Investigaciones Biomédicas del CSIC, Madrid, Spain.

PMID: 1513332
DOI: 10.1007/BF00229640

Abstract

The biochemical properties of Artemia ras proteins (p21) have been studied after immunoprecipitation with the monoclonal antibody Y13-259. The ras products bind GTP and GDP, and have GTPase activity. Artemia p21 was unable to hydrolyze Gp4G, although this dinucleotide exhibits high affinity for the protein. Our results demonstrate that the protein(s) recognized by the Y13-259 antibody in this crustacean behave as typical mammalian ras p21s.

Publication types

Research Support, Non-U.S. Gov't

MeSH terms

Animals
Artemia / chemistry*
Binding, Competitive
Dinucleoside Phosphates / metabolism
GTP Phosphohydrolases / analysis
Guanosine Triphosphate / metabolism
Precipitin Tests
Proto-Oncogene Proteins p21(ras) / chemistry*
Proto-Oncogene Proteins p21(ras) / immunology
Substrate Specificity

Substances

Dinucleoside Phosphates
diguanosine tetraphosphate
Guanosine Triphosphate
GTP Phosphohydrolases
Proto-Oncogene Proteins p21(ras)