Initiation of protein synthesis in animal mitochondria. Purification and characterization of translational initiation factor 2.

  title={Initiation of protein synthesis in animal mitochondria. Purification and characterization of translational initiation factor 2.},
  author={H. Liao and L. Spremulli},
  journal={The Journal of biological chemistry},
  volume={266 31},
Bovine liver mitochondrial translational initiation factor 2 (IF-2mt) has been purified to near homogeneity. The scheme developed results in a 24,000-fold purification of the factor with about 26% recovery of activity. SDS-polyacrylamide gel electrophoresis indicates that IF-2mt has a subunit molecular mass of 85 kDa. IF-2mt promotes the binding of formyl(f)Met-tRNA to mitochondrial ribosomes but is inactive with the nonformylated derivative. IF-2mt is active on chloroplast 30 S ribosomal… Expand
Expression, Purification, and Mechanistic Studies of Bovine Mitochondrial Translational Initiation Factor 2 (*)
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