Lysozyme volume change

Figure 4. Changes in UV absorbance of ozonized lysozyme. Volumes of 3.0 ml of O.IM buffer containing 0.59-1.11 mg lysozyme (initial amounts of protein were different) were exposed to Os/Og at 20 ml/min. Ozone delivery was 1.6 nmoles/min. Absorbance spectra were recorded at intervals and changes at 280 and 288 nm were plotted.

Sasahara, K., M. Sakurai, and K. Nitta. 1999. The volume and compressibility changes of lysozyme associated with guanidinium chloride and pressure-assisted unfolding. Journal of Molecular Biology. 291, 693. 

Lysozyme Cell-wall hydrolysis of some bacteria. Hydrolysis of 1,4 bonds between 2-acetamido-2-deoxy-) -D-glucose and / /-acetylmuramic acid Antibiotic Spectrophotometry One unit produces a change in absorbance at 450 nm of 0.001 per min at pH 6.2 and 25°C, using a suspension of Micrococcus lysodeikticus as substrate, in a 2.6 ml reaction volume (1 cm light path)... 

The conformational changes induced by high pressures are generally detected by variations in the absorption or the emission of the aromatic chromophores or of extrinsic probes such as anilino naphtalene sulfonate (ANS) bound to the protein. Recent developments of the techniques allow detection of fluorescence polarization at pressures up to 11 kbar (Chryssomalis et al, 1981). Detectable spectroscopic changes occur at pressures higher than 4 kbar for monomeric proteins. The results obtained with lysozyme indicated a reversible increase of 60% in the apparent hydro-dynamic volume between 6 and 10 kbar. A simple interpretation in terms of solvent penetration was proposed. The data obtained with chymotryp-sinogen are more difficult to interpret since aggregation occurred (Chryssomalis et al, 1981). 

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