Abstract
RIBOSOMES obtained from Escherichia coli contain ribonuclease (RNase) which is latent if the ribosome is intact1. It has been reported that this enzyme originates in the cell wall and adds to the particle only during preparation2. This finding is in contradiction to earlier work3,4 and the work of Anraku5 which suggest that the enzyme is an intrinsic part of the ribosome. The experiments of Neu et al.2 showed addition of RNase to ribosomes but no inactivation had been mentioned. If ribosomes are treated with 0.5 M ammonium chloride solution the RNase is released6,7 and subsequently separated from the ribosome by ‘Sephadex’ filtration8.
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References
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SCHELL, P. Separation and Recombination of Ribosomal Ribonuclease from Ribosomes. Nature 210, 1157–1158 (1966). https://doi.org/10.1038/2101157a0
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DOI: https://doi.org/10.1038/2101157a0
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