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Serum lysozyme

Berbamine Study of serum lysozyme levels in berbamine-in-duced macrophage activation 608... [Pg.199]

Jolles and Joll s (1984) have reviewed the use of lysozyme as a marker in certain diseases. Serum lysozyme levels have been used extensively in the diagnosis of leukemias. Jolles and Jolles discussed some of the reasons for increased and decreased serum levels in various diseases, such as acute or chronic granulocytic leukemia, myeloid metaplasia, and aplastic anemia, and decreased levels in tears in keratoconjunctivitis. They have also considered the interaction of lysozyme with sulfated proteoglycans and its role in the calcification of epiphyseal cartilage. It is to be expected that such studies will yield valuable information, giving rise to further applications in the future (see also Fett et al., 1985). Lysozyme will continue, of course, to serve as a prototype protein for the investigation of the specificity of immune recognition. [Pg.298]

Serum lysozyme/ C-reactive protein Phagocytosis/ ROS production NCC killing T/B-lymphocyte function... [Pg.240]

In mice intraperitoneally administered 50 to 450 mg/ kg of the food colorant safflower yellow daily for 8 days, a decrease in serum lysozyme concentration and phago-cytosing functions of both peritoneal macrophages and peripheral leukocytes was observed. The treatment also diminished the production of plaque-forming cells and specific rosette-forming cells, and inhibited the delayed-type hypersensitivity reaction and the activation of T suppressor cells elicited by supraoptimal immunization (Lu et al. 1991). [Pg.172]

Elevated levels of serum lysozyme have been observed in cases of Gaucher disease this high level was considered to reflect an increased body mass of reticuloendothelial cells. It was suggested that the enzyme elevation might be of use in diagnosis of Gaucher disease. In cases of monocytic leukaemia, myelomonocytic leukaemia, and myeloma no evidence has been found for immunoglobulin (IgG)-lysozyme complexes. The mobility of the serum lysozyme was identical to that of free urinary lysozyme. [Pg.456]

S. Hirano, M. Iwata, K. Yamanaka, H. Tanaka, T. Toda, and H. Inui, Enhancement of serum lysozyme activity by injecting a mixture of chitosan oligosaccharides intravenously in rabbits (biological chemistry). Agricultural and Biological Chemistry, 55 (10), 2623-2625,1991. [Pg.125]

Other data suggests effects of Se upon cells of the RES perhaps independent of GSHPx activity. Serum lysozyme has been shown to be a useful marker of macrophage mediated host response... [Pg.56]

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]

Fig. 16. Isotherms of protein bonding by nonionized CP (a = 0) /) lysozyme — MA-EDMA (2.5 mol%) copolymer 2) haemoglobin — MA-EDMA (2.5mol%) copolymer 3) haemoglobin - AA-EDMA (2.5mol%) copolymer 4) haemoglobin — MA-EDMA (2.5 mol%)gr. copolymer 5) serum albumin — MA-EDMA (2.5 mol%) copolymer. Ceq... Fig. 16. Isotherms of protein bonding by nonionized CP (a = 0) /) lysozyme — MA-EDMA (2.5 mol%) copolymer 2) haemoglobin — MA-EDMA (2.5mol%) copolymer 3) haemoglobin - AA-EDMA (2.5mol%) copolymer 4) haemoglobin — MA-EDMA (2.5 mol%)gr. copolymer 5) serum albumin — MA-EDMA (2.5 mol%) copolymer. Ceq...
Table 8. Parameters of cooperative bonding of lysozyme, haemoglobin and serum albumin (proteins) by a macroreticular MA-EDMA (2.5 mol%) copolymer... Table 8. Parameters of cooperative bonding of lysozyme, haemoglobin and serum albumin (proteins) by a macroreticular MA-EDMA (2.5 mol%) copolymer...
By adding 1-alkanols to AOT-based w/o microemulsions, some proteins (ribonucle-ase, lysozyme, alpha-chymotrypsin, pepsin, bovine serum albumin, and catalase) are readily expelled, while the major part of the surfactant remained in solution [171]. [Pg.488]

FIG. 4 Relationship between the final AOT and protein amounts in the solid phase for several different experiments, using a w/o-ME extractant of 50 or 100 mM AOT (unifilled and filled symbols, respectively), Wg = 20. Proteins (upward-pointing triangles) bovine serum albumin (downward-pointing triangles) a -ch5miotrypsin (diamonds) lysozyme. (Reprinted with permission from Ref. 58.)... [Pg.478]

Coradin, T., Coupe, A. and Livage, J. (2003) Interactions of bovine serum albumin and lysozyme with sodium silicate solutions. Cdloids and Surfaces B-Biointerfaces, 29, 189-196. [Pg.112]

LSZ lysozyme RNase ribonuclease aLA a -lactalbumin aLA(-Ca2+) Ca2+ depleted aLA BSA bovine serum albumin. [Pg.112]

Fig. 6. Plateau-values, I"P1 /mg m 2, of adsorption isotherms of lysozyme (LSZ), ribonuclease (RNase), a -lactalbumin (aLA), calcium-depleted (X -lactalbumin (aLA(-Ca )) and bovine serum albumin (BSA) on hydrophobic polystyrene (PS) and hydrophilic hematite (a — Fe203) and silica (Si02) surfaces. An indication of the charge density of the surface is given by the zeta-potential, C, and of the proteins by + and signs. Ionic strength 0.05 M T = 25°C. (Derived from Currie et al. 2003). Fig. 6. Plateau-values, I"P1 /mg m 2, of adsorption isotherms of lysozyme (LSZ), ribonuclease (RNase), a -lactalbumin (aLA), calcium-depleted (X -lactalbumin (aLA(-Ca )) and bovine serum albumin (BSA) on hydrophobic polystyrene (PS) and hydrophilic hematite (a — Fe203) and silica (Si02) surfaces. An indication of the charge density of the surface is given by the zeta-potential, C, and of the proteins by + and signs. Ionic strength 0.05 M T = 25°C. (Derived from Currie et al. 2003).
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])...
Concerning the nature and structure of such amyloid peptide or protein channels, oligomers with annular morphologies have in fact been observed by EM for a-synuclein (Lashuel et al., 2002) and equine lysozyme (Malisauskas et al., 2003) even in the absence of any lipids or membranes. Channel-like structures have also been reconstituted in liposomes and observed by SFM for A/ i 4o, A/ j 42, human amylin, a-synuclein, ABri, ADan, and serum amyloid A (Fig. 5A Lin et al., 2001 Quist et al., 2005). Doughnut-shaped structures with a diameter of 10-12 nm and a central hole size of 1-2 nm (Fig. 5B) were imaged on top of lipid membranes (Quist et al., 2005). However, the radius of curvature of the SFM tips meant that it is not possible to say whether the pores were really traversing the lipid bilayer. [Pg.227]

Patients with thermal injury are also deficient in specific granules. In this case, however, it appears that this deficit is due to activation of the cells such that they discharge their specific granules. Neutrophils from patients with bums have an increased expression of plasma-membrane markers (as would be predicted if specific-granule membranes have fused with the plasma membrane), and serum levels of lysozyme and lactoferrin are elevated. These patients have impaired chemotaxis and defective oxygen metabolism. [Pg.277]

FRET to occur, and thus no FI emission is observed. The specificity of this assay was also examined for mixed samples. The mixed lysozyme samples were prepared in fetal bovine serum (FBS), human saliva and human urine. It was found that FAM emission was still visible upon addition of each mixed sample, implying that this assay has a great potential for the detection of real biological samples. This study illuminates that introduction of specific aptamer/protein interaction as the recognition event, and utilization of FRET as the signal transduction channel, is an effective way to develop CPE-based protein sensors with good specificity. [Pg.442]


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See also in sourсe #XX -- [ Pg.55 ]




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