Name | lysozyme |
---|---|
Synonyms | LYZ; LZM; Lysozyme; Lysozyme C; Lysozyme C precursor; Lysozymes; Lysozyme Cs; Lysozyme C precursors |
Name | ethylene |
---|---|
CAS | ethene |
PubMed | Abstract | RScore(About this table) | |
---|---|---|---|
19585531 | Wang P, Tao D, Zhang L, Liang Z, Zhang Y: Microchip free flow planar reversed phase electrochromatography with monolithic stationary phase. J Sep Sci. 2009 Aug;32(15-16):2629-34. Poly (butyle methyacrylate-co-ethylene dimethacrylate) was prepared by UV-initiated polymerization in a glass microchamber (42 mm long, 23 mm wide, and 28 microm deep). Furthermore, microFF-PRPEC was also successfully applied into the separation of lysozyme and ribonuclease B, and resolution as high as 9.4 was obtained. |
1(0,0,0,1) | Details |
19505142 | Bays E, Tao L, Chang CW, Maynard HD: Synthesis of Semitelechelic Maleimide Poly (PEGA) for Protein Conjugation By RAFT Polymerization. Biomacromolecules. 2009 Jun 9. A furan-protected maleimide chain transfer agent (CTA) was employed in the RAFT polymerization of poly (ethylene glycol) methyl ether acrylate (PEGA). |
0(0,0,0,0) | Details |
19637151 | Gao G, Yan Y, Pispas S, Yao P: Sustained and extended release with structural and activity recovery of lysozyme from complexes with (sulfamate carboxylate) isoprene/ethylene oxide block copolymer. Macromol Biosci. 2010 Feb 11;10(2):139-46. |
169(2,2,2,9) | Details |
20349227 | Lee MH, Chen YC, Ho MH, Lin HY: Optical recognition of salivary proteins by use of molecularly imprinted poly (ethylene-co-vinyl /quantum dot composite nanoparticles. Anal Bioanal Chem. 2010 Mar 28. Composite QDot/MIPs were prepared using phase inversion of poly (ethylene-co-vinyl (EVAL) solutions with various ethylene mole ratios in the presence of salivary target molecules (e.g. amylase, lipase, and lysozyme). |
88(1,1,2,3) | Details |
19963219 | Moosmann A, Christel J, Boettinger H, Mueller E: Analytical and preparative separation of PEGylated lysozyme for the characterization of chromatography media. J Chromatogr A. 2010 Jan 8;1217(2):209-15. Epub 2009 Nov 17. The effect of PEGylation on cation exchange chromatography was studied with poly (ethylene glycol) of different chain lengths (5kDa, 10kDa and 30kDa) using lysozyme as a model system. |
11(0,0,1,6) | Details |
19746957 | Annunziata O, Vergara A, Paduano L, Sartorio R, Miller DG, Albright JG: Quaternary diffusion coefficients in a protein-polymer-salt-water system determined by rayleigh interferometry. J Phys Chem B. 2009 Oct 8;113(40):13446-53. Specifically, we have measured the nine multicomponent diffusion coefficients, D (ij), for the lysozyme-poly (ethylene glycol)-NaCl-water system at pH 4.5 and 25 degrees C using precision Rayleigh interferometry. |
7(0,0,1,2) | Details |
20301119 | Ganguli S, Yoshimoto K, Tomita S, Sakuma H, Matsuoka T, Shiraki K, Nagasaki Y: Improving the Heat Resistance of Ribonuclease A by the Addition of Poly (N,N-diethylaminoethyl methacrylate)-graft-poly (ethylene glycol) (PEAMA-g-PEG). Macromol Biosci. 2010 Mar 18. Poly (N,N-diethylaminoethyl methacrylate)-graft-poly (ethylene glycol) (PEAMA-g-PEG) has previously been used as a novel additive to improve the heat resistance of lysozyme, which has a positive net charge and a negatively charged active site. |
6(0,0,1,1) | Details |
19889250 | Alessandro Del Nobile M, Gammariello D, Di Giulio S, Conte A: Active coating to prolong the shelf life of Fior di latte cheese. J Dairy Res. 2010 Feb;77(1):50-5. Epub 2009 Nov 5. The active coating was prepared by dissolving, in two alginic acid solutions (5 and 8% w/v), different concentrations of lysozyme (0.25, 0.50 and 1.00 mg ml-1)+50 mm of Ethylene-Diamine Tetraacetic Acid (EDTA). |
6(0,0,1,1) | Details |
19923710 | Reis NM, Chirgadze DY, Blundell TL, Mackley MR: The effect of protein-precipitant interfaces and applied shear on the nucleation and growth of lysozyme crystals. Acta Crystallogr D Biol Crystallogr. 2009 Nov;65(Pt 11):1127-39. Epub 2009 Oct 22. In the presence of the water-soluble polymer poly (ethylene glycol) (PEG) a sharp interface was observed to form immediately within the drop, giving an initial clear separation between the lighter protein solution and the heavier precipitant. |
4(0,0,0,4) | Details |
19717157 | Krenkova J, Gargano A, Lacher NA, Schneiderheinze JM, Svec F: High binding capacity surface grafted monolithic columns for cation exchange chromatography of proteins and peptides. J Chromatogr A. 2009 Oct 2;1216(40):6824-30. Epub 2009 Aug 18. Poly (glycidyl methacrylate-co-ethylene methacrylate) monoliths have been prepared in 100 microm i.d. capillaries and their epoxy groups hydrolyzed to obtain poly (2,3-dihydroxypropyl methacrylate-co-ethylene methacrylate) matrix. A mixture of ovalbumin, alpha-chymotrypsinogen, cytochrome c, ribonuclease A and lysozyme was used to assess the chromatographic performance for large molecules while a cytochrome c digest served as a model mixture of peptides. |
2(0,0,0,2) | Details |
19527757 | Censi R, Vermonden T, van Steenbergen MJ, Deschout H, Braeckmans K, De Smedt SC, van Nostrum CF, di Martino P, Hennink WE: Photopolymerized thermosensitive hydrogels for tailorable diffusion-controlled protein delivery. J Control Release. 2009 Dec 16;140(3):230-6. Epub 2009 Jun 13. The hydrogels consist of ABA triblock copolymer, in which the thermosensitive A-blocks are methacrylated poly (N-(2-hydroxypropyl) methacrylamide lactate) s and the B-block is poly (ethylene glycol) with molecular weight of 10 kDa. It was demonstrated that the release rate of three model proteins (lysozyme, BSA and IgG, with hydrodynamic diameters ranging from 4.1 to 10.7 nm) depended on the protein size and hydrogel molecular weight between cross-links and was governed by the Fickian diffusion. |
2(0,0,0,2) | Details |
20095560 | Brandl F, Hammer N, Blunk T, Tessmar J, Goepferich A: Biodegradable hydrogels for time-controlled release of tethered peptides or proteins. Biomacromolecules. 2010 Feb 8;11(2):496-504. Hydrogels were prepared by step-growth polymerization of branched poly (ethylene glycol). Using FITC-BSA and lysozyme as model proteins, we showed the potential of the developed hydrogels for time-controlled release. |
1(0,0,0,1) | Details |
19812821 | Holyst R, Bielejewska A, Szymanski J, Wilk A, Patkowski A, Gapinski J, Zywocinski A, Kalwarczyk T, Kalwarczyk E, Tabaka M, Ziebacz N, Wieczorek SA: Scaling form of viscosity at all length-scales in poly (ethylene glycol) solutions studied by fluorescence correlation spectroscopy and capillary electrophoresis. Phys Chem Chem Phys. 2009 Oct 28;11(40):9025-32. Epub 2009 Aug 3. Additionally, for the smallest probes (rhodamine B and lysozyme) we have verified, using capillary electrophoresis and fluorescence correlation spectroscopy, that the Stokes-Einstein (SE) relation holds, providing that we use a size-dependent viscosity in the formula. |
1(0,0,0,1) | Details |
20200599 | Mehrotra S, Lynam D, Maloney R, Pawelec KM, Tuszynski MH, Lee I, Chan C, Sakamoto J: Time Controlled Protein Release from Layer-by-Layer Assembled Multilayer Functionalized Agarose Hydrogels. Adv Funct Mater. 2010 Jan 22;20(2):247-258. Alternatively, here it is shown that pH-responsive H-bonded poly (ethylene glycol)(PEG)/poly (acrylic acid)(PAA)/protein hybrid layer-by-layer (LbL) thin films, when prepared over agarose, provided sustained release of protein under physiological conditions for more than four weeks. Lysozyme, a protein similar in size and isoelectric point to BDNF, is released from the multilayers on the agarose and is biologically active during the earlier time points, with decreasing activity at later time points. |
1(0,0,0,1) | Details |
20063358 | Yao C, Qi L, Yang G, Wang F: Preparation of sub-micron skeletal monoliths with high capacity for liquid chromatography. J Sep Sci. 2010 Mar;33(4-5):475-83. A novel kind of poly (glycidyl methacrylate-co-ethylene glycol dimethacrylate)-based monolithic column was developed for LC by directing supramolecular self-assembly of high internal phase emulsion. Separation of proteins mixture (cytochrome c, myoglobin, ribonuclease A, lysozyme and BSA) on the monolith was achieved within 4 min at velocity of 1440.0 cm/h. |
1(0,0,0,1) | Details |
19517430 | Salim M, Wright PC, McArthur SL: Studies of electroosmotic flow and the effects of protein adsorption in plasma-polymerized microchannel surfaces. Electrophoresis. 2009 Jun;30(11):1877-87. This paper presents a study of EOF properties of plasma-polymerized microchannel surfaces and the effects of protein (fibrinogen and lysozyme) adsorption on the EOF behavior of the surface-modified microchannels. |
1(0,0,0,1) | Details |
20099804 | Spross J, Sinz A: A capillary monolithic trypsin reactor for efficient protein digestion in online and offline coupling to ESI and MALDI mass spectrometry. Anal Chem. 2010 Feb 15;82(4):1434-43. Trypsin was immobilized on a poly (glycidyl methacrylate-co-acrylamide-co-ethylene glycol dimethycrylate) monolith using the glutaraldehyde technique. Digestion efficiencies of the IMER were evaluated using model proteins and protein mixtures as well as chemically cross-linked lysozyme regarding the addition of denaturants and increasing digestion temperature. |
1(0,0,0,1) | Details |
19746967 | Tai H, Howard D, Takae S, Wang W, Vermonden T, Hennink WE, Stayton PS, Hoffman AS, Endruweit A, Alexander C, Howdle SM, Shakesheff KM: Photo-cross-linked hydrogels from thermoresponsive PEGMEMA-PPGMA-EGDMA copolymers containing multiple methacrylate groups: mechanical property, swelling, protein release, and cytotoxicity. Biomacromolecules. 2009 Oct 12;10(10):2895-903. In this study, water-soluble thermoresponsive copolymers containing multiple methacrylate groups were synthesized via one-step deactivation enhanced atom transfer radical polymerization (ATRP) of poly (ethylene glycol) methyl ether methacrylate (PEGMEMA, M (n) = 475), poly methacrylate (PPGMA, M (n) = 375), and ethylene glycol dimethacrylate (EGDMA) and were used to form covalent cross-linked hydrogels by photopolymerization. Release studies using lysozyme as a model protein demonstrated a sustained release profile that varied dependent on the copolymer composition, cross-linking density, and the temperature. |
1(0,0,0,1) | Details |
20298865 | Sun X, Liu R, He X, Chen L, Zhang Y: Preparation of phenylboronic acid functionalized cation-exchange monolithic columns for protein separation and refolding. Talanta. 2010 May 15;81(3):856-64. Epub 2010 Jan 25. In this study, we described a simple and effective modification procedure to prepare poly (methacrylate-co-ethylene glycol dimethacrylate) monolithic columns functionalized with 3-aminophenylboronic acid. The chromatographic performance of the cation-exchange monolith was evaluated through separating a mixture of five proteins such as lysozyme, cytochrome c, ribonuclease A, trypsin and bovine serum albumin and one-step purification of lysozyme from egg whites, and the expected results were obtained. |
1(0,0,0,1) | Details |
19619398 | Lee BS, Yoon OJ, Cho WK, Lee NE, Yoon KR, Choi IS: Construction of protein-resistant pOEGMA films by helicon plasma-enhanced chemical vapor deposition. J Biomater Sci Polym Ed. 2009;20(11):1579-86. This paper describes the formation of protein-resistant, poly (ethylene glycol) methyl ether methacrylate (pOEGMA) thin films by helicon plasma-enhanced chemical vapor deposition (helicon-PECVD). pOEGMA was successfully grafted onto a substrate, as a model substrate, without any additional surface initiators, by plasma polymerization of OEGMA. To investigate the protein-resistant property of the pOEGMA films, four different proteins, bovine serum albumin, fibrinogen, lysozyme and ribonuclease A, were tested as model proteins for ellipsometric measurements. |
1(0,0,0,1) | Details |
19674784 | Aimetti AA, Machen AJ, Anseth KS: Poly (ethylene glycol) hydrogels formed by thiol-ene photopolymerization for enzyme-responsive protein delivery. Biomaterials. 2009 Oct;30(30):6048-54. Epub 2009 Aug 12. Lastly, the bioactivity of lysozyme was maintained above 90% following the exposure to thiol-ene photopolymerization conditions. |
1(0,0,0,1) | Details |
19630008 | Chen X, Tolley HD, Lee ML: Polymeric strong cation-exchange monolithic column for capillary liquid chromatography of peptides and proteins. J Sep Sci. 2009 Aug;32(15-16):2565-73. The monolith had a dynamic binding capacity of approximately 52 mg/mL of column volume for lysozyme and cytochrome C. |
1(0,0,0,1) | Details |