Purification and characterization of a germ cell-specific form of elongation factor 1 alpha (EF-1 alpha) from Xenopus laevis

J Morales; O Mulner-Lorillon; H Denis; R Bellé

doi:10.1016/0300-9084(91)90011-o

Purification and characterization of a germ cell-specific form of elongation factor 1 alpha (EF-1 alpha) from Xenopus laevis

Biochimie. 1991 Sep;73(9):1249-53. doi: 10.1016/0300-9084(91)90011-o.

Authors

J Morales¹, O Mulner-Lorillon, H Denis, R Bellé

Affiliation

¹ Laboratoire de Physiologie de la Reproduction, Université P et M Curie, INRA, UA CNRS 1449, Paris, France.

PMID: 1747390
DOI: 10.1016/0300-9084(91)90011-o

Abstract

Elongation factor 1 alpha (EF-1 alpha) was purified to homogeneity from full-grown oocytes of Xenopus laevis. This protein is encoded by a gene previously shown to be expressed in male and female germ cells, and repressed in somatic cells. The purified protein was identified with EF-1 alpha on criteria of molecular mass, cross-reaction with antibodies raised against Artemia salina EF-1 alpha, affinity for guanine nucleotides, and ability to promote the mRNA-dependent binding of aminoacyl tRNA to 80S ribosomes.

Publication types

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

MeSH terms

Adenosine Triphosphate / metabolism
Animals
Binding Sites
Cell Division
Electrophoresis, Polyacrylamide Gel
Guanosine Diphosphate / metabolism
Guanosine Triphosphate / metabolism
Immunoblotting
Molecular Weight
Oocytes / chemistry*
Peptide Elongation Factor 1
Peptide Elongation Factors / chemistry
Peptide Elongation Factors / isolation & purification*
Peptide Elongation Factors / metabolism
RNA, Transfer, Phe / metabolism
Xenopus laevis

Substances

Peptide Elongation Factor 1
Peptide Elongation Factors
RNA, Transfer, Phe
Guanosine Diphosphate
Guanosine Triphosphate
Adenosine Triphosphate