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- W1591691145 abstract "A study has been made of the effect of salts on the assay for lysozyme (mucopeptide N-acetylmuramylhydrolase, EC 3.2.1.17) in which the decrease in turbidity of a suspension of lyophilized Micrococcus lysodeikticus is measured. Determinations were carried out in the presence of several types of salts in the concentration range of 5–500 mM and the pH range 5–10. Lysozyme is inactive in distilled water, is activated by low concentrations of salt and is inhibited by high concentrations of salt. Analysis of the data shows that the activation at low salt concentration is most closely correlated with a non-specific ionic strength effect and that the inhibition at high salt concentration is most closely correlated with cationic concentration and charge. At a given ionic strength, polyvalent cations are stronger inhibitors than monovalent cations. The effect of cations changes with pH such that the optimal cation concentration decreases with increasing pH. For example, 50 mM monovalent cation is optimal at pH 7.0, but at pH 9.0 it is strongly inhibitory. Thus, the activity of lysozyme cannot be adequately represented by a pH-activity curve, but it is necessary to establish an activity-pH cation profile." @default.
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- W1591691145 date "1971-02-01" @default.
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- W1591691145 title "Studies on the structure and function of lysozyme" @default.
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- W1591691145 doi "https://doi.org/10.1016/0005-2795(71)90210-8" @default.
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