The activity of initiation factors obtained from free and membrane-bound polyribosomes of liver and of transplantable H5123 hepatoma of rats was investigated by using an assay of protein synthesis in vitro in which poly (U)-directed polyphenylalanine synthesis was measured. Initiation factors of membrane-bound polyribosomes prepared by using the anionic detergent deoxycholate exhibited less activity in incorporating [14C]phenylalanyltRNA into polypetides than did initiation factors of free polyribosomes. However, when membrane-bound polyribosomes were prepared after using the non-ionic detergent Triton X-100, no significant differences in activities in polyphenylalanine synthesis were observed between the initiation factors of free and membrane-bound polyribosomes. These results suggest that Triton X-100 is preferable to deoxycholate in the isolation of of initiation factors from polyribosomes. Initiation factors, prepared by using Triton X-100, of free polyribosomes of hepatoma exhibited greater activity in the stimulation of polyphenylalanine synthesis than did the initiation factors of free or membrane-bound polyribosomes of host livers or of membrane-bound polyribosomes of hepatomas.
Research Article|October 01 1975
Initiation factors in protein synthesis by free and membrane-bound polyribosomes of liver and hepatoma
C N Murty;
Biochem J (1975) 152 (1): 143-151.
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C N Murty, E Verney, H Sidransky; Initiation factors in protein synthesis by free and membrane-bound polyribosomes of liver and hepatoma. Biochem J 1 October 1975; 152 (1): 143–151. doi: https://doi.org/10.1042/bj1520143
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