![]() Lysozyme hydrochloride structure
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Common Name | Lysozyme hydrochloride | ||
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CAS Number | 9066-59-5 | Molecular Weight | N/A | |
Density | N/A | Boiling Point | N/A | |
Molecular Formula | N/A | Melting Point | N/A | |
MSDS | USA | Flash Point | N/A |
Sequential separation of lysozyme, ovomucin, ovotransferrin, and ovalbumin from egg white.
Poult. Sci. 93(4) , 1001-9, (2014) Ovalbumin, ovotransferrin, ovomucin, and lysozyme are a few of the egg white proteins that can be used as functional components. The objective of this study was to develop a simple, sequential separation method for multiple proteins from egg white. Separated ... |
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Refolding of SDS-denatured proteins using amphipathic cosolvents and osmolytes.
Curr. Protoc. Protein Sci. Chapter 28 , Unit28.5, (2013) Currently, the investigation of protein refolding processes involves several time-consuming stages that require large amounts of protein and costly chemicals. Consequently, there is great interest in developing new approaches to the study of protein renaturat... |
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Functional display of active tetrameric beta-galactosidase using Bacillus subtilis spore display system.
J. Nanosci. Nanotechnol. 13(3) , 2313-9, (2013) For the functional bacterial surface display of active enzyme of multimeric form, which is generally impossible due to molecular assembly of the monomer subunit subsequent to the secretion of displayed target protein outside the cell, a new surface display sy... |
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Genetically encoded click chemistry for single-molecule FRET of proteins.
Methods Cell Biol. 113 , 169-87, (2013) Single molecule Fluorescence Resonance Energy Transfer (FRET) has been widely applied to study structure, function and dynamics of complex biological systems. Labeling of proteins at specific positions with fluorescent dyes is a challenging and key step for a... |
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An RNA aptamer possessing a novel monovalent cation-mediated fold inhibits lysozyme catalysis by inhibiting the binding of long natural substrates.
RNA 20(4) , 447-61, (2014) RNA aptamers are being developed as inhibitors of macromolecular and cellular function, diagnostic tools, and potential therapeutics. Our understanding of the physical nature of this emerging class of nucleic acid-protein complexes is limited; few atomic reso... |
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Reentrant liquid-liquid phase separation in protein solutions at elevated hydrostatic pressures.
Phys. Rev. Lett. 112(2) , 028101, (2014) We present results from small-angle x-ray scattering data on the effect of high pressure on the phase behavior of dense lysozyme solutions in the liquid-liquid phase separation region, and characterize the underlying intermolecular protein-protein interaction... |
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Curcumin and kaempferol prevent lysozyme fibril formation by modulating aggregation kinetic parameters.
Biochim. Biophys. Acta 1844(3) , 670-80, (2014) Interaction of small molecule inhibitors with protein aggregates has been studied extensively, but how these inhibitors modulate aggregation kinetic parameters is little understood. In this work, we investigated the ability of two potential aggregation inhibi... |
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Investigation on the interaction between cyclophosphamide and lysozyme in the presence of three different kind of cyclodextrins: determination of the binding mechanism by spectroscopic and molecular modeling techniques.
Molecules 18(1) , 789-813, (2013) The interactions between cyclophosphamide (CYC) and lysozyme (LYZ) in the presence of different cyclodextrins (CDs) were investigated by UV absorption, fluorescence spectroscopy, circular dichroism (CD), and molecular modeling techniques under imitated physio... |
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A role for IRF8 in B cell anergy.
J. Immunol. 191(12) , 6222-30, (2013) B cell central tolerance is a process through which self-reactive B cells are removed from the B cell repertoire. Self-reactive B cells are generally removed by receptor editing in the bone marrow and by anergy induction in the periphery. IRF8 is a critical t... |
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Inelastic X-ray scattering studies of the short-time collective vibrational motions in hydrated lysozyme powders and their possible relation to enzymatic function.
J. Phys. Chem. B 117(4) , 1186-95, (2013) High-resolution inelastic X-ray scattering was used to investigate the collective vibrational excitations in hydrated lysozyme powders as a function of hydration level and temperature. It is found that the samples with strong enzymatic function are "soft", in... |