Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: EC:3.2.1.17 (lysozyme)
 21,489 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

The preparation of a stable affinity medium with heparin as the affinity ligand has been investigated. Glyceryl controlled-pore glass (CPG) was activated with 1-cyano-4-dimethylaminopyridinium tetrafluoroborate and coupled with heparin. This affinity medium was used to separate some simple proteins, trypsinogen and lysozyme, in a high-performance liquid chromatographic configuration. The heparin-glyceryl-CPG was also used to separate alpha- and beta-lipoproteins in human serum. The effectiveness of the separation is confirmed by radial immunodiffusion and the determination of the cholesterol content of each of the separated fractions.
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PMID:Preparation of heparin-glyceryl controlled-pore glass affinity media for the separation of alpha- and beta-lipoproteins. 156 91

This study was conducted to assess the relative accuracy of five different assay techniques for the determination of protein concentration in human mixed saliva. The protein concentration of paraffin-stimulated saliva from 20 individuals was determined using the biuret reaction, the Lowry assay, a modified Lowry technique using bicinchoninic acid, and two dye-binding assays. Using bovine serum albumin as the standard, mean values ranged from 0.67 to 2.37 mg/ml. The use of bovine serum albumin, trypsinogen, lysozyme, bovine pancreatic ribonuclease, and poly-L-lysine as standards with the five different assay techniques to measure protein concentration of pooled mixed saliva from the above subjects produced results ranging from 0.74 to 65.5 mg/ml. The protein concentration obtained for this saliva sample by amino acid analysis was consistent with the value obtained for the biuret reaction using any of the five different standard proteins. Thus, the protein concentration obtained for human saliva depends upon both the technique used and the protein standard.
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PMID:Comparison of five techniques for the determination of protein content in mixed human saliva. 382 22

It is found that for nearly all the proteins under study, the value of 1/P0', cut off on the ordinate by the extrapolation of the dependencies 1/P = f(T/eta . /tau B), is larger than the value of 1/P0 for model compounds--tryptophan, N-acetyltryptophan, glycyl-tryptophan. It is shown, that this may indicate the existence both of high-frequence intramolecular mobility, with the relaxation time rho much less than tau, and low-frequency intramolecular mobility the magnitude rho of which is of the same order as tau, independent on the medium viscosity. This peculiarity in the interpretation of the data, received by the method of rotational depolarization of UV-fluorescence of proteins arises because some tryptophan residues within the macromolecules of proteins are not accessible to the molecules of the solvent and that is why the rotational relaxation time of their intramolecular mobility is not dependent on the viscosity of the solvent. It is indicated that intramolecular mobility is inherent in tryptophan residues both with short wave and long wave spectrum of UV-fluorescence. The relaxation time, measured by the method of fluorescence depolarization, appeared to be smaller than that calculated for the short axe of an equivalent ellipsoid of revolution for a series of proteins (lysozyme, trypsin, pepsin, bovin serum albumin in acid medium, myelin basic protein). This indicates the existence of intramolecular mobility the magnitude rho of which is of the same order as tau dependent on the solvent viscosity in these proteins. Zymogens--trypsinogen and pepsinogen do not have such intramolecular mobilities.
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PMID:[Polarization of intrinsic fluorescence of proteins. III. Intramolecular submobility of tryptophan residues]. 662 23

Capillary zone electrophoresis (CZE) of five model proteins (lysozyme, myoglobin, ribonuclease A, alpha-lactalbumin, and trypsinogen), using ammonium formate as the electrophoretic buffer and triethylamine (TEA) as a buffer additive at pH 2.5, was used for protein separation. The electrophoretic behavior of these proteins was examined with respect to various concentrations (10-40 mM) of TEA and of ammonium formate. Based on the experimental parameters of electrophoretic resolution, current, and peak separation time, an electrolyte (30 mM each of TEA and ammonium formate) was empirically derived as the optimum for scale-up separation. The loading limit for proteins, covering a wide range of injection volumes (60-990 nl) and amount of protein (1-21 pmol of each protein), was investigated on 75 and 100 microns I.D. untreated fused-silica capillaries. Protein adsorption (average < 15%) was experimentally determined using this volatile buffer system.
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PMID:Optimization of the capillary zone electrophoresis loading limit and resolution of proteins, using triethylamine, ammonium formate and acidic pH. 914 Jul 59

Quantifying the diffusive transport of large molecules in avascular cartilage tissue is important both for planning potential pharamacological treatments and for gaining insight into the molecular-scale structure of cartilage. In this work, the diffusion coefficients of gadolinium-DTPA and Gd-labeled versions of four proteins-lysozyme, trypsinogen, ovalbumin, and bovine serum albumin (BSA) with molecular weights of 14,300, 24,000, 45,000, and 67,000, respectively-have been measured in healthy and degraded calf cartilage. The experimental technique relies on the effect of the paramagnetic on the relaxation properties of the surrounding water, combined with the time course of a 1-dimensional spatial profile of the water signal in the cartilage sample. The enhanced technique presented here does not require a prior measurement of the relaxivity of the paramagnetic compound in the sample of interest. The data are expressed as the ratio of the diffusion coefficient of a compound in cartilage to its diffusion coefficient in water. For healthy cartilage, this ratio was 0.34 +/- 0.07 for Gd-DTPA, the smallest compound, and fell to 0.3 +/- 0.1 for Gd-lysozyme, 0.08 +/- 0.04 for Gd-trypsinogen, and 0.07 +/- 0.04 for Gd-ovalbumin. Gd-BSA did not appear to enter healthy cartilage tissue beyond a surface layer. After the cartilage had been degraded by 24-h trypsinization, these ratios were 0.60 +/- 0.03 for Gd-DTPA, 0.40 +/- 0.08 for Gd-lysozyme, 0.42 +/- 0.09 for Gd-trypsinogen, 0.16 +/- 0.14 for Gd-ovalbumin, and 0.11 +/- 0.05 for Gd-BSA. Thus, degradation of the cartilage led to increases in the diffusion coefficient of up to fivefold for the Gd-labeled proteins. These basic transport parameters yield insights on the nature of pore sizes and chemical-matrix interactions in the cartilage tissue and may prove diagnostically useful for identifying the degree and nature of damage to cartilage.
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PMID:Diffusion of paramagnetically labeled proteins in cartilage: enhancement of the 1-D NMR imaging technique. 1113 85

The vacuum ultraviolet circular dichroism (VUVCD) spectra of 15 globular proteins (myoglobin, hemoglobin, human serum albumin, cytochrome c, peroxidase, alpha-lactalbumin, lysozyme, ovalbumin, ribonuclease A, beta-lactoglobulin, pepsin, trypsinogen, alpha-chymotrypsinogen, soybean trypsin inhibitor, and concanavalin A) were measured in aqueous solutions at 25 degrees C in the wavelength region from 260 to 160 nm under a high vacuum, using a synchrotron-radiation VUVCD spectrophotometer. The VUVCD spectra below 190 nm revealed some characteristic bands corresponding to different secondary structures. The contents of alpha-helices, beta-strands, turns, and unordered structures were estimated using the SELCON3 program with VUVCD spectra data on the 15 proteins. Prediction of the secondary-structure contents was greatly improved by extending the circular dichroism spectra to 165 nm. The numbers of alpha-helix and beta-strand segments calculated from the distorted alpha-helix and beta-strand contents did not differ greatly from those obtained from X-ray crystal structures. These results demonstrate that synchrotron-radiation VUVCD spectroscopy is a powerful tool for analyzing the secondary structures of proteins.
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PMID:Secondary-structure analysis of proteins by vacuum-ultraviolet circular dichroism spectroscopy. 1511 39

This paper describes the photosynthesis of gold nanoparticles (GNPs) in the presence of bovine serum albumin (BSA). The concentration of NaAuCl4 and the relative ratio of NaAuCl4 to BSA are important parameters for controlling the size of the GNPs. We prepared GNPs having average diameters ranging from 7 to 50 nm by illumination (Hg-Xe lamp) of phosphate-buffered solutions (pH 3.0-11.0) containing 1 mM NaAuCl4 and 10 microM BSA for 9 h. The size distribution of the GNPs synthesized at pH 7.0 is narrower relative to that of those prepared at other values of pH. Based on the observation that there are no GNPs formed at 25 degrees C in the absence of either BSA or illumination, we conclude that photolytic reduction is the main mechanism for the formation of the GNPs and that BSA acts as a capping agent to stabilize the as-synthesized GNPs. In addition to BSA, several other proteins, such as beta-casein, conalbumin, hemoglobin, beta-lactoglobulin, lysozyme, myoglobin, ovalbumin, pepsin, and trypsinogen play the same role.
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PMID:Photosynthesis of gold nanoparticles in presence of proteins. 1643 Jan 51

An atmospheric molding protocol has been used to prepare an ionic methacrylate-based copolymer sample support chips for MALDI (pMALDI)-MS by targeting selected groups of various monomers copolymerized during molding, namely, carboxy, sulfo, dimethylalkyamino, and trimethylalkylammonium groups. The new disposable array chips provide analyte-oriented enhancement of protein adsorption to the modified substrates without requiring complicated surface coating or derivatization. The MALDI-MS performance of the new ionic copolymer chips was evaluated for lysozyme, beta-lactoglobulin A, trypsinogen and carbonic anhydrase I using washing with solutions prepared in pH or ionic strength steps. On cationic chips, the proteins are washed out at pH lower than their p/ values, and on anionic chips at pH higher than their p/ values. The ability of the microfabricated pMALDI chip set to selectively adsorb different proteins from real samples and to significantly increase their MS-signal was documented for the transmembrane photosystem I protein complex from the green alga Chlamydomonas reinhardtii. The proteins were almost exclusively adsorbed according to calculated pI values and grand average of hydropathy (GRAVY) indexes. The new disposable chips reduce manipulation times and increase measurement sensitivity for real-world proteomic samples. The simple atmospheric molding procedure enables additional proteomic operations to be incorporated on disposable MALDI-MS integrated platforms.
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PMID:Atmospheric molding of ionic copolymer MALDI-TOF/MS arrays: a new tool for protein identification/profiling. 1710 78

The ability to form amyloid fibrils from a wide range of proteins would open up the opportunity to augment studies of the molecular basis of amyloid fibril formation. We investigated 36 different conditions with respect to four model proteins to evaluate their ability to form amyloid fibrils. In a 5% ethanol solution at pH 2 at 57 degrees C, hen egg white lysozyme, bovine beta-lactoglobulin, and bovine trypsinogen formed mature-type fibrils, while only histone H2A formed immature-type fibrils. Under these conditions, 25 of the 38 proteins formed amyloid fibrils. In addition, three additional proteins formed fibrils in a solution containing 5% trifluoroethanol instead of 5% ethanol. In summary, a total 28 proteins formed amyloid fibrils. Under these extreme conditions, chemical fragmentation was observed. Destabilization of the native structure, strengthening of hydrogen bonds, and chemical fragmentation are thought to play important roles in the formation of amyloid fibrils.
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PMID:Systematic analysis of aggregates from 38 kinds of non disease-related proteins: identifying the intrinsic propensity of polypeptides to form amyloid fibrils. 1748 39

The structural effect induced by therapeutic ultrasound on proteins in aqueous solution has been investigated with FTIR spectroscopy, UV-VIS spectroscopy, circular dichroism and light scattering. Six proteins (cytochrome, lysozyme, myoglobin, bovine serum albumin, trypsinogen, and alpha-chymotrypsinogen A) with different molecular weight and secondary structure have been studied. The experiment has been performed using an ultrasound source at resonant frequency of 1 MHz and sonication times of 10, 20, 30, 40, 50, and 60 min. A different behaviour of proteins under sonication depends on the dominant secondary structure type (alpha-helix or beta-sheets) and on the grade of the ordered structure. The results suggest that the free radicals, produced by water sonolysis, have an important role in the changes of structural order.
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PMID:Structural changes induced in proteins by therapeutic ultrasounds. 1927 7


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