Gene/Protein Disease Symptom Drug Enzyme Compound
Pivot Concepts: Gene/Protein Disease Symptom Drug Enzyme Compound   Target Concepts: 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)

A strong cation-exchange separation material has been prepared from monodisperse divinylbenzene particles modified by a "grafting to" approach, utilizing as anchoring points epoxy groups introduced onto the surface of the particles via oxidation of residual vinyl groups. The grafted chains consisted of thiol-terminated telomers of sulfopropyl methacrylate prepared by iniferter mediated polymerization, and grafting was performed by reaction of the corresponding thiolate anion with the surface epoxy groups. Attachment through epoxy moieties that were subsequently converted into 2,3-propanediol groups increased the hydrophilicity of the polymeric particles and incubation experiments showed no signs of the proteins denaturing on the column during an extended contact time of 1 h at room temperature. The performance of the grafted material was demonstrated by the chromatographic separation of cytochrome C, lysozyme, myoglobin, and ribonuclease A, in a cation-exchange mode.
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PMID:A cation-exchange material for protein separations based on grafting of thiol-terminated sulfopropyl methacrylate telomers onto hydrophilized monodisperse divinylbenzene particles. 1861 33

Nonlinear adsorption plays an important role in determining the chromatographic behavior of proteins in preparative ion-exchange chromatography. In this article, the steric mass action (SMA) isotherm is used in conjunction with a mass transport model to describe nonlinear cation-exchange chromatography. Excellent agreement is observed between simulated and experimental step gradient separations of the proteins alpha-chymotryp-sinogen A, cytochrome C, and lysozyme. A systematic method of selecting the optimum step gradient program for a given separation problem is presented and employed to study optimization of step gradient chromatography under conditions of high mass loading. This article includes consideration of the effects of the adsorption properties of the feed stream, the feed stream concentration, protein solubility, and otherconstraints on the optimum separation conditions.(c) John Wiley & Sons, Inc.
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PMID:Optimization of step gradient separations: Consideration of nonlinear adsorption. 1862 11

A neutral octadecyl monolithic (ODM) column for RP capillary electrochromatography (RP-CEC) has been developed. The ODM column was prepared by the in situ polymerization of octadecyl acrylate (ODA) as the monomer and trimethylolpropanetrimethacrylate (TRIM) as the crosslinker, in a ternary porogenic solvent containing cyclohexanol, ethylene glycol, and water. The ODM column exhibited cathodal EOF over a wide range of pH and ACN concentration in the mobile phase despite the fact that it was devoid of any fixed charges. It is believed that the EOF is due to the adsorption of ions from the mobile phase onto the surface of the monolith thus imparting to the neutral ODM column the zeta potential necessary to support the EOF required for mass transport across the monolithic column. Furthermore, the adsorption of mobile phase ions to the neutral monolith modulated solute retention and affected the separation selectivity. The wide applications of the neutral ODM column were demonstrated by its ability to separate a wide range of small and large solutes, both neutral and charged. While the separation of the neutral solutes was based on RP retention mechanism, the charged solutes were separated on the basis of their electrophoretic mobility and hydrophobic interaction with the C18 ligands of the stationary phase. As a typical result, the neutral monolithic column was able to separate peptides quite rapidly with a separation efficiency of nearly 200,000 plates/m, and this efficiency was exploited in tryptic peptide mapping of standard proteins, e. g., lysozyme and cytochrome C, by isocratic elution.
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PMID:Neutral octadecyl monolith for reversed phase capillary electrochromatography of a wide range of solutes. 1869 9

An HPLC-resonance Rayleigh scattering (RRS) (HPLC-RRS) detection system is described for separation and detection of proteins. This system is based on the modification of a commercial HPLC instrument involving the addition of a pump and a T-shaped interface, and a common fluorescence detector was used for detection. The detection principle is based on the change of RRS intensity of the ion-association complex formed from biebrich scarlet (BS) and protein. The RRS signal was detected at lambdaex=lambdaem=376 nm. The utility of the presented method was demonstrated by the separation and determination of four proteins involving cytochrome (Cyt-c), lysozyme (Lys), HSA, and gamma-globulin (gamma-Glo). An LOD of 0.2-1.0 microg/mL was reached and a linear range was found between peak area and concentration in the range of 0.20-3.0 microg/mL for Cyt-c, 0.25-2.5 microg/mL for Lys, 1.5-10 microg/mL for HSA, and 2.0-15 microg/mL for gamma-Glo, with linear regression coefficients all above 0.99. The method presented has been applied to determine HSA and gamma-Glo in human serum samples synchronously.
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PMID:Resonance Rayleigh scattering for detection of proteins in HPLC. 1870 97

A method for the fast separation of human serum and enrichment of low abundance proteins was developed using offline 2D liquid chromatography (2D-LC) consisted of chromatographic cake (10 mm x 20 mm i. d.) and reversed-phase liquid chromatography (RPLC). The protein after separation and enrichment was detected using matrix assisted laser desorption/ ionization time of flight mass spectrometry (MALDI-TOF MS). This method was validated by four standard proteins at very low concentration. It was found that the detection limits were 1 pmol/microL for the enriched cytochrome-c and myoglobin, and 0.1 pmol/microL for enriched lysozyme and insulin. This method has been applied to the proteomic research of human serum, and it was found that the signal intensity and the number of detected proteins/peptides in MALDI-TOF MS increased with the increase of the loading sample volume of the human serum on chromatographic cake. A total of 285 fractions (M(r) < 15 000) were found when 1.0 mL serum sample was loaded on the chromatographic cake. In addition, cytochrome-c in low abundance was also separated and enriched successfully when 1 microg cytochrome-c was added into 0.5 mL original serum. The results showed that 2D-LC consisting of the chromatographic cake and RPLC was successfully applied to not only the fast separation and preparation of human serum sample with large loading volume in one cycle of analysis, but also the efficient isolation and enrichment of the lower abundance proteins/peptides in human serum. Moreover, it successfully increased the detection efficiency of the low abundance proteins/peptides in human serum with MALDI-TOF MS.
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PMID:[Fast separation and preparation of proteomics samples of human serum using high performance hydrophobic interaction chromatographic cake]. 1872 70

We describe an approach that uses surface plasmon resonance (SPR) spectroscopy and self-assembled monolayers (SAMs) for the high-throughput screening of ligands for use in displacement and affinity chromatographic processes. We identified a set of commercially available organic amines and allowed them to react with SAMs presenting interchain carboxylic anhydride groups; the resulting surfaces presented ligands of interest in a background of carboxylic acid groups. We used SPR spectroscopy to determine the extent of adsorption of two model proteinslysozyme and cytochrome conto these "multimodal" surfaces and to select promising "affinity" ligands for further characterization. The attachment of selected ligands to UltraLink Biosupport resulted in beads with a significantly greater affinity for lysozyme than for cytochrome c that would be suitable for use in affinity chromatographic processes. Furthermore, we also used the screens to design "affinity displacers"small molecules that selectively retain lysozyme on chromatographic resins, while displacing cytochrome c. The combination of SPR spectroscopy and SAMs represents a powerful technique for identifying novel ligands that enable the purification of complex protein mixtures.
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PMID:Surface plasmon resonance spectroscopy-based high-throughput screening of ligands for use in affinity and displacement chromatography. 1878 66

This work reports the advantages of a label free electrochemical aptasensor for the detection of lysozyme. The biorecognition platform was obtained by the adsorption of the aptamer on the surface of a carbon paste electrode (CPE) previously blocked with mouse immunoglobulin under controlled-potential conditions. The recognition event was detected from the decrease in the guanine and adenine electro-oxidation signals produced as a consequence of the molecular interaction between the aptamer and lysozyme. The biosensing platform demonstrated to be highly selective even in the presence of large excess (9-fold) of bovine serum albumin, cytochrome C and myoglobin. The reproducibility for 10 repetitive determinations of 10.0 mg L(-1) lysozyme solution was 5.1% and 6.8% for guanine and adenine electro-oxidation signals, respectively. The detection limits of the aptasensor were 36.0 nmol L(-1) (if considering guanine signal) and 18.0 nmol L(-1) (if taking adenine oxidation current). This new sensing approach represents an interesting and promising alternative for the electrochemical quantification of lysozyme.
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PMID:Label-free electrochemical aptasensor for the detection of lysozyme. 1917 27

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

A strong cation-exchange (SCX) monolithic stationary phase was prepared in 75 microm id capillaries by direct in situ polymerization of sulfopropyl methacrylate and polyethylene glycol diacrylate in a ternary porogen system consisting of methanol, cyclohexanol, and water. The resulting monolith exhibited good dynamic binding capacity, fast kinetic adsorption of proteins, and high permeability. The monolith had a dynamic binding capacity of approximately 52 mg/mL of column volume for lysozyme and cytochrome C. The monolith was evaluated for SCX capillary LC of synthetic peptides, natural peptides, and protein standards. Fast separation of proteins was achieved in less than 4 min. The average peak capacity for peptides was 28 using a relatively steep gradient when hydrophobic interactions were suppressed with 40% acetonitrile.
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PMID:Polymeric strong cation-exchange monolithic column for capillary liquid chromatography of peptides and proteins. 1963 8

In order to improve the stationary phase retention of polar solvent systems and aqueous two-phase systems (ATPSs), we designed a multiple spiral disk assembly for type-J high-speed counter-current chromatography (HSCCC). The stationary phase retention was studied under different elution modes by using two solvent systems that contained 1-butanol-acetic acid-water (4:1:5, V/V/V) and polyethylene glycol (PEG) 1000-K2HPO4-water (12.5:12.5:75, W/W/W). The best retention was obtained in L-I-T, U-O-H, L-I-H three modes by pumping lower mobile phase from inner terminal (I) to outer terminal (O), and upper mobile phase from outer terminal (O) to inner terminal (I) at a relatively high flow rate. Meanwhile, the relationship between retention percentage of the stationary phase (Sf) and various parameters such as flow-rate (F), rotation speed (w) and column temperature (T) was also studied. Sf increased with the increase of w and decreased with the increase of F. Regression analysis showed a linear relationship between Sf and F1/2/w. The influence of T on Sf was not obvious between 20 degrees C and 40 degrees C, lower temperature than 20 degrees C was not suitable for viscous ATPSs. Acceptable resolutions were achieved when it was applied for the separation of dipeptides including Leu-Tyr and Val-Tyr by using 1-butanol-acetic acid-water (4:1:5, V/V/V) solvent system. The proteins including cytochrome C and myoglobin, lysozyme and myoglobin, and fresh chicken egg-white proteins were well separated by 12.5% PEG1000-12.5% K2HPO4-75% water (pH 9.0) and 16% PEG 1000-12.5% K2HPO4-71.5% water (pH 8.0) system.
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PMID:[Application of spiral disk column in high-speed counter-current chromatography for peptide and protein separation]. 1963 41


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