Purification and characterization of a germ cell-specific form of elongation factor 1 alpha (EF-1 alpha) from Xenopus laevis.
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.
Morales
J
J
Laboratoire de Physiologie de la Reproduction, Université P et M Curie, INRA, UA CNRS 1449, Paris, France.
Mulner-Lorillon
O
O
Denis
H
H
Bellé
R
R
D000255:Adenosine Triphosphate / Q000378:metabolism; D000818:Animals; D001665:Binding Sites; D002455:Cell Division; D004591:Electrophoresis, Polyacrylamide Gel; D006153:Guanosine Diphosphate / Q000378:metabolism; D006160:Guanosine Triphosphate / Q000378:metabolism; D015151:Immunoblotting; D008970:Molecular Weight; D009865:Oocytes / Q000737:chemistry*; D020648:Peptide Elongation Factor 1; D010445:Peptide Elongation Factors / Q000737:chemistry / Q000302:isolation & purification* / Q000378:metabolism; D012360:RNA, Transfer, Phe / Q000378:metabolism; D014982:Xenopus laevis
D020648:Peptide Elongation Factor 1; D010445:Peptide Elongation Factors; D012360:RNA, Transfer, Phe; D006153:Guanosine Diphosphate; D006160:Guanosine Triphosphate; D000255:Adenosine Triphosphate