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Lysozyme molecular weight

Figure 5. Repelling voltage curves for electrosprayed solution of lysozyme (molecular weight 14,600) in three parts ethanol to one part water by volume. Curve 4 is the repelling voltage curve for electrosprayed solvent only, drawn to the same scale (7). Figure 5. Repelling voltage curves for electrosprayed solution of lysozyme (molecular weight 14,600) in three parts ethanol to one part water by volume. Curve 4 is the repelling voltage curve for electrosprayed solvent only, drawn to the same scale (7).
Albumin, from bovine serum (BSA, molecular weight 66 kDa, V fraction), lysozyme (molecular weight 14.3 kDa), poly(ethylene glycol) methyl ether methacrylate (PEGMA475, average M - 475 g.mor , Aldrich), 2-(dimethylamino)ethyl methacrylate (DMAEMA, Aldrich, 99%) and... [Pg.80]

Three different types of columns packed with gels of different pore sizes are available. Columns should be selected that are suitable for the molecular weight range of specific samples, as each type has a different exclusion limit (Fig. 6.41, page 215). Bovine serum albumin (BSA), myoglobin, and lysozyme show good peak shapes using only 100 mM of sodium phosphate buffer as an eluent. There is no need to add any salt to the eluent to reduce the ionic interaction between protein and gel. [Pg.205]

Figure 14.3 SDS-PAGE of recovery of lysozyme in the presence of BME. Lane M, molecular weight marker lane 1, FFPE lysozyme tissue surrogate lane 2, a 75 mg/mL solution of lysozyme heat coagulated for 10 min at 100°C in 10 mM sodium phosphate buffer, pH 7.4. Both preparations were resuspended in 20mM Tris-HCl, pH 4, with 2% SDS and 0.5 M BME, and heated at 100°C for 20min followed by a cycle of heating at 60°C for 2h. For more detail, see Reference 25. Figure 14.3 SDS-PAGE of recovery of lysozyme in the presence of BME. Lane M, molecular weight marker lane 1, FFPE lysozyme tissue surrogate lane 2, a 75 mg/mL solution of lysozyme heat coagulated for 10 min at 100°C in 10 mM sodium phosphate buffer, pH 7.4. Both preparations were resuspended in 20mM Tris-HCl, pH 4, with 2% SDS and 0.5 M BME, and heated at 100°C for 20min followed by a cycle of heating at 60°C for 2h. For more detail, see Reference 25.
Figure 14.4 Gel image of proteins extracted from a mixed carbonic anhydrase lysozyme tissue surrogate. Lane M, molecular weight marker lane 1, a 1 2 mol ratio mixture of native, non-formalin-treated carbonic anhydrase and lysozyme lane 2, mixed surrogate with 1 2 mol ratio carbonic anhydrase lysozyme, solubilized and retrieved in 20mM Tris-HCl, pH 4.0, with 2% SDS lane 3, mixed surrogate with 1 2 mol ratio carbonic anhydrase lysozyme, solubilized and retrieved in 20mM Tris-HCl, pH 6.0, with 2% SDS. Protein bands corresponding to lysozyme monomer (a), carbonic anhydrase monomer (b), and the putative lysozyme-carbonic anhydrase heterodimer (c) are indicated. For more detail, see Reference 25. Figure 14.4 Gel image of proteins extracted from a mixed carbonic anhydrase lysozyme tissue surrogate. Lane M, molecular weight marker lane 1, a 1 2 mol ratio mixture of native, non-formalin-treated carbonic anhydrase and lysozyme lane 2, mixed surrogate with 1 2 mol ratio carbonic anhydrase lysozyme, solubilized and retrieved in 20mM Tris-HCl, pH 4.0, with 2% SDS lane 3, mixed surrogate with 1 2 mol ratio carbonic anhydrase lysozyme, solubilized and retrieved in 20mM Tris-HCl, pH 6.0, with 2% SDS. Protein bands corresponding to lysozyme monomer (a), carbonic anhydrase monomer (b), and the putative lysozyme-carbonic anhydrase heterodimer (c) are indicated. For more detail, see Reference 25.
The model systems, discussed here, contain one type of well-defined protein and one type of well-characterized solid surface in an aqueous medium containing one type of low molecular-weight electrolyte. Table 2 summarizes some relevant properties of the proteins. Lysozyme (LSZ)... [Pg.111]

Fig. 3 SDS-PAGE Photograph Separation (Lane Mr and A) and activity staining (Lane B and C) of the crude filtrate of Funalia trogii. Lane Mr standard molecular weight markers ([3-galactosi-dase, 118.0 kDa bovine serum albumin, 79.0 kDa ovalbumin, 47.0 kDa carbonic anhydrase, 33.0 kDa P-lactoglobulin, 25.0 kDa and lysozyme, 19.5 kDa). Relative mobilities of the standard markers vs. common logarithms of their molecular masses were plotted.With the linear regression output, the molecular masses of the proteins in the crude filtrate were estimated (taken from [18])... Fig. 3 SDS-PAGE Photograph Separation (Lane Mr and A) and activity staining (Lane B and C) of the crude filtrate of Funalia trogii. Lane Mr standard molecular weight markers ([3-galactosi-dase, 118.0 kDa bovine serum albumin, 79.0 kDa ovalbumin, 47.0 kDa carbonic anhydrase, 33.0 kDa P-lactoglobulin, 25.0 kDa and lysozyme, 19.5 kDa). Relative mobilities of the standard markers vs. common logarithms of their molecular masses were plotted.With the linear regression output, the molecular masses of the proteins in the crude filtrate were estimated (taken from [18])...
D-Lysine, systematic name, formula, and molecular weight, 2 556t DL-Lysine, systematic name, formula, and molecular weight, 2 556t L-Lysine, systematic name, formula, and molecular weight, 2 556t Lysocellin, 20 120, 137 Lysozyme... [Pg.539]

Cojocel, C., Dociu, N., Maita, K., Sleight, S.D. and Hook, J.B. (1983). Effects of aminoglycosides on glomerular permeability, tubular reabsorption, and intracellular catabolism of the cationic low molecular weight protein lysozyme. Toxicol. Appl. Pharm. 39 129-139. [Pg.678]

Example ESI on a magnetic sector instrument set to R = 20,000 allows for the flail resolution of isotopic peaks in case of medium-molecular weight proteins (Fig. 11.21). This enables the direct determination of the charge state of the ions from the spacing of the isotopic peaks, i.e., 1 1h- for the lysozyme ion due to the average spaces of Am = 0.091 u and 13h- for the myoglobin ion due to Am = 0.077 u. In this particular case, the lysozyme [M+llH]" ion serves as a mass reference for the accurate mass measurement of the unknown" [M+13H] ion. [103]... [Pg.460]

Fig.44 (left) Dry thickness (in nm) of a poly(2-hydroxyethyl methacrylate) (PHEMA) brush in an orthogonal gradient as a function of the PHEMA grafting density and molecular weight The scale represents the thickness of dry polymer (in nm). (right) Adsorbed amount of lysozyme as a fimction of the position on the orthogonal PHEMA gradient. The scale represents the fluorescence intensity (in a.u.). (Reproduced with permission from [164])... [Pg.115]

Fig. 2.1. Semilogarithmic plot of molecular weight (Mr) of marker proteins vs relative mobility (Rf) of marker proteins in gels of different acrylamide concentrations %T. Proteins 1 aprotinin (6.5 kD) 2 lysozyme (14.5 kD) 3 soybean trypsin inhibitor (21.5 kD) 4 carbonic acid anhydrase (31 kD) 5 hen ovalbumin (45 kD) 6 bovine serum albumin (66 kD) 7 phosphorylase b (97.4 kD) 8 8-galactosidase (116 kD) 9 myosin (205 kD)... Fig. 2.1. Semilogarithmic plot of molecular weight (Mr) of marker proteins vs relative mobility (Rf) of marker proteins in gels of different acrylamide concentrations %T. Proteins 1 aprotinin (6.5 kD) 2 lysozyme (14.5 kD) 3 soybean trypsin inhibitor (21.5 kD) 4 carbonic acid anhydrase (31 kD) 5 hen ovalbumin (45 kD) 6 bovine serum albumin (66 kD) 7 phosphorylase b (97.4 kD) 8 8-galactosidase (116 kD) 9 myosin (205 kD)...
Isophorone produced kidney effects in male rats in the NTP (1986) study. Strasser (1988) found that isophorone caused protein droplet formation in the kidneys of male rats, suggesting that isophorone can induce protein nephropathy. Alden (1986) discussed the possibility that proteinuric humans and humans with low molecular weight protein nephropathy, such as people with multiple myeloma (Bence-Jones protein) or mononuclear cell leukemia (lysozyme), may be more susceptible to chemically-induced protein nephropathy. He concluded, however, that this syndrome is probably specific to the male rat. [Pg.59]

As with X-ray crystallography, as the molecular weight of the molecule increases, the difficulties in performing structural studies increase. The lanthanide probe method has so far been applied in great detail to only one protein, lysozyme.5 The nuclei studied were protons. Because of the complexity of the protein nmr spectrum, it was necessary to apply techniques to resolve and simplify the spectrum and to assign the observed resonances to specific nuclei in the molecule. Table III lists some details of these methods, with references. [Pg.64]


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See also in sourсe #XX -- [ Pg.9 ]

See also in sourсe #XX -- [ Pg.82 , Pg.83 ]

See also in sourсe #XX -- [ Pg.7 , Pg.360 ]




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