H Lysozyme

Fig. 3. Cation-exchange chromatography of protein standards. Column poly(aspartic acid) Vydac (10 pm), 20 x 0.46 cm. Sample 25 pi containing 12.5 pg of ovalbumin and 25 pg each of the other proteins in the weak buffer. Flow rate 1 ml/min. Weak buffer 0.05 mol/1 potassium phosphate, pH 6.0. Strong buffer same +0.6 mol/1 sodium chloride Elution 80-min linear gradient, 0-100% strong buffer. Peaks a = ovalbumin, b = bacitracin, c = myoglobin, d = chymotrypsinogen A, e = cytochrom C (reduced), / = ribonuclease A, g = cytochrome C (oxidised), h = lysozyme. The cytochrome C peaks were identified by oxidation with potassium ferricyanide and reduction with sodium dithionite [47]...

The diamagnetic susceptibility is a measure of the averaged electronic distribution in bulk matter. Careri et al. (1977, 1980) showed that the differential diamagnetic susceptibility per gram of water adsorbed on lysozyme powders reached the bulk water value at 0.2 h. Lysozyme behaved as a normal diamagnetic substance. The diamagnetic susceptibility and the enthalpy of sorption for lysozyme change similarly at low hydration. 

Gonzalez R, Albericio F, Cascone O, Iannucci NB (2010) Improved antimicrobial activity of h-lysozyme (107-115) by rational Ala substitution. J Peptide Sci 16 424-429... 

McKenzie, H.A., White jr., F.H. Lysozyme and a-lact-albumin Structure, function, and interrelationships. Adv. Protein Chem. 41, 174 (1991)... 

Hayward, S., Kitao, A., Berendsen, H.J.C. Model-free methods to analyze domain motions in proteins from simulation A comparison of normal mode analysis and molecular dynamics simulation of lysozyme. Proteins 27 (1997) 425-437. 

Fremont, D.H., Monnaie, D., Nelson, C.A., Hendrickson, W.A., Unanue, E.R. Crystal structure of I-A in complex with a dominant epitope of lysozyme. Immunity 8 305-317, 1998. 

Figure 17.5 Diagram of the T4 lysozyme stmcture showing the iocations of two mutations that stabilize the protein stmcture by providing eiectrostatic interactions with the dipoles of a helices. (Adapted from H. Nicholson et al.. Nature 336 651-656, 1988.)...

Faber, H.R., Matthews, B.W. A mutant T4 lysozyme displays five different crystal conformations. Nature 348 263-266, 1990. 

Continuous free flow electrophoresis has been used for the separation of biopolymers (e.g. ovalbumin and lysozyme) [20] as well as smaller inorganic species (e.g. [Co sepulchrate)] and [Co (CN)g] ) [21]. Sample processing rates of 15 mg h were reported for a mixture of Amaranth (MW 804) and Patent Blue VF (MW 1159) [22]. 

Figure 12.9 MALDI-TOF mass spectrum of chicken egg-white lysozyme. The peak at 14,307.7578 daltons (amu) is due to the monoprotonated protein, M+H+, and that at 28,614.2188 daltons is due to an impurity formed by dimerization of the protein. Other peaks are various protonated species, M+H rH ...

Petrovskii, A., Loiko, N., Nikolaev, Yu., Kozlova, A., El -Registan, G., Deryabin, D., Mikhailenko, N., Kobzeva, T., Kanaev, P., Krupyanskii, Yu. Regulation of the function activity of lysozyme by alkylhydroxybenzenes. Microbiology, Vol.78, No.2, (March 2009), pp. 144-153, ISSN 1350-0872 Reusch, R., Sadoff, H. Novel lipid components of the Azotobacter vinelandii cyst membrane. 

To check if PemB is surface exposed, E. chrysanthemi cells were subjected to proteolysis. Treatment of the cell suspension with trypsin, proteinase K or chimotrypsin at a concentration of 0.1 to 1 mg/ml for 1 h did not cause PemB proteolysis or its liberation into the medium. Cell pre-treatment with EDTA-lysozyme, which renders the periplasmic proteins accessible to proteases, gave no effect. PemB was also resistant to proteolytic digestion in extract of cells disrupted by sonication or in a French press. Only addition of Triton X-100 (up to 0.1%) causing formation of the micelles with PemB lead to a quick proteolyis of this protein (data not shown). In another approach to analyse the PemB exposition, bacterial cells were labelled with sulfo-NHS-biotin. This compound is unable to cross membranes and biotinylation... 

Anderson DE, Hurley JH, Nicholson H, Baase WA, Mathews BW Hydro-phobic core repacking and aromatic-aromatic interaction in the thermostable mutant of T4 lysozyme Ser 117-Phe. Protein Sci 1993 2 1285-1290. 

It has been suggested recently that PPII helix may be the killer conformation in such diseases (Blanch et al., 2000). This was prompted by the observation, described in Section III,B, of a positive band at 1318 cm-1, not present in the ROA spectrum of the native state, that dominates the ROA spectrum of a destabilized intermediate of human lysozyme (produced by heating to 57°C at pH 2.0) that forms prior to amyloid fibril formation. Elimination of water molecules between extended polypeptide chains with fully hydrated 0=0 and N—H groups to form... 

K. Koizumi, M. Tachibana, H. Kawamoto, and K. Kojima, Temperature Dependence of Microhardness of Tetragonal Hen-egg-white Lysozyme Single Crystals, Phil. Mag., 84,2961 (2004). 

COOH groups of the PE (PAA or PGA) and the -NH2 moieties of the pre-loaded protein, using l-ethyl-3-(3-dimethylaminopropyl) carbodiimide hydrochloride (EDC) as a catalyst [99]. Negligible enzyme desorption (<0.1 %) is observed from cross-linked lysozyme-loaded MS spheres after exposing the samples to an aqueous solution for 48 h, while about 25 % of the immobilized lysozyme is desorbed under the same conditions when the lysozyme is not cross-linked. 

Tomizawa H, Yamada H, Wada K, et al. Stabilization of lysozyme against irreversible inactivation by suppression of chemical reactions. J. Biochem. (Tokyo) 1995 117 635-640. 

Yamada, H., Imoto, T., Fujita, K., Okazaki, K., and Motomura, M. (1981) Selective modification of aspartic acid-101 in lysozyme by carbodiimide reaction. Biochemistry 20, 4836M842. 

Voss, J., Salwinski, L., Kaback, H. R., and Hubbell, W. L. (1995) A method for distance determination in proteins using a designed metal ion binding site and site-directed spin labeling evaluation with T4 lysozyme. Proc. Natl. Acad. Sci. USA 92,12295-12299. 

Warshel, A. and Levitt, H. Theoretical studies of enzymatic reactions dielectric, electrostatic and steric stabilization of the carbonium ion in the reaction of lysozyme, J. Mol. Biol., 103 (1976), 227-249... 

The effect of ozone on lysosomal enzymes has been studied by a number of investigators. Ozone has been clearly shown to inactivate lysozyme in vitro, but the effects of inhaled ozone on the activity of lysozyme appear to depend on the pulmonary fraction under study. Holzman et al. reported that exposure of rabbits or mice to ozone resulted in a decrease in the lysozyme activity of bronchopulmonary lavage samples. The effect was linearly related to product of ozone concentration and duration of exposure, although relatively high concentrations of ozone (2.0-S.S ppm) were used in this acute-exposure experiment (1-4 h). The authors also reported that alveolar cells present in the bronchial lavage of rabbits exposed to ozone at 10 ppm for 3 h had a decrease in the rate of lysosomal... 

Similarly, Chow et al. observed an increase in the lysozyme activity of a soluble lung fraction and of plasma after continuous exposure of rats to ozone at 0.8 ppm for 8 days. However, no difference in lung or plasma lysozyme activity from control values was present in rats continuously exposed to 0.2 or 0.5 ppm or intermittently exposed (0.2-0.8 ppm, 8 h/day for 7 days). Histochemical evidence of an increase in lung acid phosphatase, a lysosomal enzyme, has also been reported. ... 

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