Amino acid incorporation into proteins by various fractions of
Pasteurella multocida was examined
and the following results were obtained.
1) Among the ribosomal fractions the components which migrated faster to the cathode in zone
electrophoresis were relatively active in amino acid incorporation, and the remainders were less active.
2) The incorporation of C
14-leucine into proteins by ribosomes was found without the addition of
supernatant fluid. This reaction was not dependent upon the addition of ATP and ATP generators and
GTP, not prevented by ribonuclease or chloramphenicol, and proceeded at 0°C at the rate of about 60 per
cent of full activity. The majority of C
14-leucine were incorporated into the inner part of peptide chains.
3) The incorporation of a small amount of C
14-leucine into proteins was found by the addition of
supernatant fluid. From various observations it is suggested that this reaction was not the incorporation into
the internal linkage of peptide chains due to the synthesis of peptides.
4) The ribosomes had 68 S of sedimentation coefficient at the presence of 0.01M magnesium ion. In
contrast with the above finding, the ribosomes prepared in the absence of magnesium ion and dialyzed against
the buffer not containing magnesium ion were separated into two subunits, having a 25.6 S and 46.6 S of
sedimentation coefficient respectively. The treatment of ribosomes prepared in the absence of magnesium ion
with 0.1M EDTA led to the substantial disappearance of ribosomes and subunits.
5) The ribosomes were composed of 42.3 per cent of protein, 35.2 per cent of ribonucleic acid, 19.9
per cent of chloroform-methanol extractable substance and 0.6 per cent of polysaccharide.
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