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JBC, Vol. 251, Issue 18, 5551-5557, Sep, 1976
W. M. Kemper, K. W. Berry and W. C. Merrick
The active protein components of initiation factor M2B (IF-M2B) have been
resolved into two homogeneous factors. These proteins, IF-M2Balpha and
IF-M2Bbeta, were purified 300- and 500-fold, respectively, with a yield of
about 15% of the original starting activity. The low molecular weight
(approximately 17,000) of these two proteins is in contrast with the much
greater molecular weights that have been found for other initiation
factors. IF-M2Balpha is also unique among the initiation factors in that it
contains no tryptophan and is capable of self-association. Both proteins
are required for model assays which utilize 40 S and 60 S subunits
(poly(U)-directed polyphenylalanine synthesis or AUG-directed
methionyl-puromycin synthesis). IF-M2Bbeta has been shown to be required
for hemoglobin synthesis, however, the presence of high concentrations of
IF-M2Balpha in the 100,000 X g lysate supernatant has precluded the
demonstration of an IF-M2Balpha requirement in hemoglobin synthesis.
Purification and properties of rabbit reticulocyte protein synthesis initiation factors M2Balpha and M2Bbeta
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