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.

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