Year: 1954
Type: article
Abstract: I954separated from TMV by treatment with sodium dodecyl sulphate was unstable, and other proteins also are more easily denatured after separation from their prosthetic groups.The presence of undegraded nucleic acid in solution with serum albumin has been found (Greenstein & Hoyer, 1950) to increase the thermal stability of the latter.Many anomalies appear when the kinetics of the fission of TMV by alkali and the subsequent destruction of the liberated nucleic acid are studied.The results were partly systematized by Gregoire (1950), who found that 0*033N sodium hydroxide acting for 4 min.at 180 split TMV into at least three products: protein that could be precipitated at pH 5*2 along with a little nucleic acid, nucleic acid which could be precipitated by hydrochloric acid along with a little protein, and a substance, which remained in the acid solution, that could catalyse the conversion of TMV nucleic acid into material not precipitated by hydrochloric acid.This action takes place in 0-033N sodium hydroxide during a few hours and the advantage of using 0-5N sodium hydroxide in the conventional methods for making nucleic acid is not that this strength of alkali is needed for the fission but that it is needed to suppress the secondary loss of acid precipitability.The high concentrations of strontium nitrate that are present when it is used to bring about fission would make it difficult to recognize any similar mechanism if it were playing a part here.But the possibility that TMV undergoes fission more readily than the other nucleoproteins because of the presence of other catalytic substance in it must be kept in mind in further work.SUMMARY 1. Tobacco mosaic virus is split at room temperature into denatured protein and free nucleic acid by solutions of strontium nitrate if the concentration of the latter is greater than molar.2. Other nucleoproteins are less easily split in this way and other related salts are not so efficient as strontium nitrate.3. Nucleic acid is decomposed by more intense treatment.
Source: Biochemical Journal
DOI: 10.1042/bj0560086
Authors: R. Bird, R. H. Hopkins
Institution: University of Birmingham
Language: English
Subfield: Biotechnology
Domain: Life Sciences
Open Access status: bronze
OpenAlex ID: W1783993237