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- W1489976609 abstract "1. The action of lysozyme on cell walls has been studied by following the reduction in turbidity of cell-wall suspensions and the liberation of reducing substances. Turbidity reduction by lysozyme has a broad pH optimum at 6.5–7.0 in 0.1 M phosphate buffer. The liberation of reducing substances by lysozyme showed an optimum at pH 7.0 when the effect of pH was studied with 0.1 M acetate and phosphate buffers over the range pH 4–8; marked discontinuities occured in changing from acetate to phosphate buffer. There was no discontinuity in the pH curves for buffers of ionic strength (μ) 0.1 and the pH optimum for liberation of reducing substances coincided with the optimum for turbidity reduction at pH 6.5. There is a parallel course for the liberation of reducing substances and turbidity reduction. 2. Ultracentrifugal analysis has shown that the higher molecular weight fragments of lysozyme-digested walls are of the order of 10,000–20,000 molecular weight. The non-dialysable fragments account for 50–70% of the original cell-wall mass. Electrophoresis of the non-dialysable fractions has shown a minimum of three electrophoretic components for M. lysodeikticus and S. lutea; B. megaterium fraction showed two electrophoretic components. These components possess high negative mobilities. 3. The major “small fragment” liberated by lysozyme action on cell walls of three lysozyme-sensitive bacteria was a substance giving the reactions of an acetylamino sugar. It behaved as an acidic substance on electrophoresis on paper at pH 6.4. Hydrolysis of this substance yielded a mixture of glucosamine and an unidentified substance giving the reactions of an amino sugar." @default.
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- W1489976609 date "1956-12-01" @default.
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- W1489976609 title "Studies of the bacterial cell wall" @default.
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- W1489976609 doi "https://doi.org/10.1016/0006-3002(56)90060-9" @default.
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