muramidase has been researched along with imidazole* in 10 studies
10 other study(ies) available for muramidase and imidazole
Article | Year |
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Insights into the Protein Ruthenation Mechanism by Antimetastatic Metallodrugs: High-Resolution X-ray Structures of the Adduct Formed between Hen Egg-White Lysozyme and
The pharmacological profile of medicinally relevant Ru(III) coordination compounds has been ascribed to their interactions with proteins, as several studies have provided evidence that DNA is not the primary target. In this regard, numerous spectroscopic and crystallographic studies have indicated that the Ru(III) ligands play an important role in determining the metal binding site, acting as the recognition element in the early stages of the protein-complex formation. Herein, we present a series of near-atomic-resolution X-ray crystal structures of the adducts formed between the antimetastatic metallodrug imidazolium Topics: Antineoplastic Agents; Cell Line, Tumor; Crystallography, X-Ray; Humans; Imidazoles; Metal-Organic Frameworks; Models, Molecular; Muramidase; Neoplasm Metastasis; Protein Conformation; Ruthenium | 2021 |
Reactions of cisplatin and cis-[PtI
Quite surprisingly, cisplatin and cis-[PtI Topics: Amino Acids; Ammonia; Antineoplastic Agents; Cisplatin; Cytochromes c; Imidazoles; Models, Molecular; Muramidase; Organoplatinum Compounds; Protein Binding; Spectrometry, Mass, Electrospray Ionization | 2020 |
Specific inhibitors of lysozyme and peptidases inhibit the growth of the rumen protozoan Entodinium caudatum without decreasing feed digestion or fermentation in vitro.
Experiments were designed to determine the effects of different chemical inhibitors of lysozyme and peptidases on rumen protozoa and the associated prokaryotes, and in vitro fermentation using Entodinium caudatum as a model protozoan species.. Imidazole (a lysozyme inhibitor), phenylmethylsulphonyl fluoride (PMSF, a serine peptidase inhibitor) and iodoacetamide (IOD, a cysteine peptidase inhibitor) were evaluated in vitro both individually and in two- and three-way combinations using E. caudatum monocultures with respect to their ability to inhibit the protozoan and their effect on feed digestion, fermentation and the microbiota. All the three inhibitors, both individually and in combination, decreased E. caudatum counts (P < 0·001), and IOD and its combinations with the other inhibitors significantly (P < 0·01) decreased ammonia concentration, with the two- and three-way combinations showing additive effective. Feed digestion was not affected, but fermentation and microbial diversity were affected mostly by PMSF, IOD and their combinatorial treatments potentially due to the overgrowth of Streptococcus luteciae accompanying with the disappearance of host ciliates.. Entodinium caudatum depends on lysozyme and peptidase for digestion and utilization of the engulfed microbes and specific inhibition of these enzymes can inhibition E. caudatum without adversely affecting feed digestion or fermentation even though they changed the microbiota composition in the cultures.. The peptidase inhibitors may have the potential to be used in controlling rumen protozoa to improve ruminal nitrogen utilization efficiency. Topics: Ammonia; Animals; Ciliophora; Digestion; Enzyme Inhibitors; Fermentation; Imidazoles; Iodoacetamide; Microbiota; Muramidase; Phenylmethylsulfonyl Fluoride; Protease Inhibitors; Rumen | 2019 |
Immobilization of lysozyme proteins on a hierarchical zeolitic imidazolate framework (ZIF-8).
A hierarchical zeolitic imidazolate framework-8 (micro/meso-ZIF-8) was fabricated by using cetyltrimethylammonium bromide as a structure-controlling agent and l-histidine as co-templates. Compared to the conventional microporous ZIF-8 (micro-ZIF-8), the hierarchical porous structure of micro/meso-ZIF-8 contains micropores and maximum mesopores of around 35.6 nm. The as-prepared hierarchical micro/meso-ZIF-8 featured a large surface area and superior spontaneous adsorption activity than micro-ZIF-8 towards lysozyme (LZM), bovine hemoglobin (BHb) and bovine serum albumin (BSA), and the adsorption capacity increased with the decreasing of the protein size due to the molecule cutoff effects. The maximum adsorption capacity of LZM on micro/meso-ZIF-8 was higher than most of the reported results under similar adsorption conditions. The analyses of adsorption kinetics and thermodynamics implied that the adsorption mechanism mainly involved physical adsorption. Moreover, the micro/meso-ZIF-8 showed good thermal stability against temperature and excellent regeneration ability in the recycling adsorption experiments. This work proposed herein opens a broad application prospect of hierarchical MOFs in biological molecule separation, immobilization and enrichment. Topics: Animals; Cattle; Enzymes, Immobilized; Hemoglobins; Imidazoles; Micrococcus; Models, Molecular; Muramidase; Protein Conformation; Serum Albumin, Bovine; Surface Properties; Zeolites | 2017 |
Novel bis(5-methyltetrazolium)amine ligand-bonded stationary phase with reduced leakage of metal ions in immobilized metal affinity chromatography of proteins.
Immobilized metal affinity chromatography (IMAC) has been widely used for the specific separation of biopolymers. However, leakage of metal ions from IMAC adsorbents is of concern in IMAC. In this study, we designed a novel tridenate bis(5-methyltetrazolium)amine (BMTA) to reduce the leakage of metal ions by improving the affinity to immobilized metal ions. The ligand was bonded onto silica via three-step reaction to prepare a high-performance IMAC stationary phase. The chromatographic behaviors of ribonuclease A, cytochrome c, and lysozyme on the Cu(II)-, Ni(II)-, and Zn(II)-chelated stationary phase were investigated with respect to pH effect and elution with an imidazole gradient. The retention times of these three proteins increased by increasing the pH of the mobile phase but decreased by increasing the concentration of the competitive displacer. The retaining strength of the three proteins on the chelated stationary phase were in the order Cu(II) > Ni(II) > Zn(II). The behavior of these three proteins was consistent with the properties of a typical IMAC. The BMTA ligand exhibited a much stronger affinity for Cu(II) and Ni(II) than iminodiacetic acid (IDA), which is often regarded as a standard tridentate IMAC ligand. Quantum mechanical calculations at the B3LYP/6-31G level were used to image the coordination mode of the protein-metal ions-BMTA complex. In addition, a fused histidine-tagged cecropin b-human epidermal growth factor (CB-EGF) from Escherichia coli crude extract was purified by the Ni(II)-chelated stationary phase, and the purity of the CB-EGF was determined to be at least 90 %. These results suggest that the BMTA ligand may have potential applications in the preparation of therapeutics. Graphical Abstract A novel ligand of tridenate bis(5-methyltetrazolium)amine (BMTA) was designed to reduce the leakage of metal ions from the column in immobolized metal affinity chromatography (IMAC). Topics: Adsorption; Chromatography, Affinity; Copper; Cytochromes c; Epidermal Growth Factor; Humans; Hydrogen-Ion Concentration; Imidazoles; Imino Acids; Muramidase; Nickel; Quantum Theory; Ribonuclease, Pancreatic; Silicon Dioxide; Tetrazolium Salts; Zinc | 2016 |
Study of the applicability of non-conventional aqueous two-phase systems in counter-current and centrifugal partition chromatography.
Aqueous two-phase systems composed of imidazolium-based ionic liquids and phosphate salts were evaluated for their applicability in liquid-liquid chromatography. The influence of the nature of ionic liquid anion and cation on the partitioning of bovine serum albumin, lysozyme and myoglobin was investigated. A mixture of K2HPO4 and KH2PO4 in a ratio of 1.82:1 wt/wt was used in all of the tested biphasic systems to adjust the pH to a range of 7-8. The results show that more hydrophobic cations decrease the partition coefficients of the proteins in the biphasic systems and outweigh the effect of the anion on the distribution of the macromolecules. Viscosities and densities of the biphasic systems were in a suitable range for liquid-liquid chromatography. Even though the partition coefficients were too high for a conventional batch operation mode, these aqueous two-phase systems show favorable properties for protein capturing in liquid-liquid chromatographic columns. Additionally, the possible application of ionic liquids as modifiers in polyethylene glycol (PEG)-based aqueous two-phase systems was investigated. It could be demonstrated that ionic liquids alter the partition coefficients of the proteins. Topics: Animals; Cattle; Centrifugation; Countercurrent Distribution; Hydrophobic and Hydrophilic Interactions; Imidazoles; Ionic Liquids; Muramidase; Myoglobin; Polyethylene Glycols; Serum Albumin, Bovine; Viscosity; Water | 2015 |
Improvement on the crystallization of lysozyme in the presence of hydrophilic ionic liquid.
The crystallization of lysozyme with hydrophilic ionic liquid 1,3-butylimidazolium chloride (BBimCl) as an additive was investigated with hanging-drop vapor diffusion crystallization protocol. The elevated threshold to super-saturation caused by the increased solubility of lysozyme in the presence of BBimCl and the slower super-saturation process of lysozyme induced by the negligible vapor pressure of BBimCl contributed to a lower super-saturation degree, offering a promoted ambient circumstance for nucleation and providing a controlled velocity for the growth of lysozyme crystal. These eventually offer a prominent promotion to the crystallization of lysozyme, i.e., less crystal polymorphism and precipitation while larger crystals and significantly improved the tolerance to the concomitant impurities or sample matrices for the crystallization of lysozyme. Therefore, the presence of BBimCl enables the direct crystallization of lysozyme from a real complex sample matrix, i.e., egg-white, which opens a promising avenue for the development of protein crystallization methodology with ionic liquids as an additive and offers vast potentials for the practical separation/purification of proteins of interest from complex real sample matrices. Topics: Crystallization; Crystallography, X-Ray; Imidazoles; Ionic Liquids; Muramidase; Protein Structure, Tertiary | 2010 |
Half-sandwich arene ruthenium(II)-enzyme complex.
The 1.6 [Angstrom] X-ray crystal structure of [(eta(6)-p-cymene)Ru(lysozyme)Cl(2)], the first of a half-sandwich complex of a protein, shows selective ruthenation of Nepsilon of the imidazole ring of His15. Topics: Arginine; Aspartic Acid; Crystallography, X-Ray; Histidine; Imidazoles; Models, Chemical; Multienzyme Complexes; Muramidase; Organometallic Compounds; Proteins; Ruthenium | 2004 |
Singlet oxygen generation by Photofrin in homogeneous and light-scattering media.
The singlet oxygen quantum yield (phi delta) for Photofrin solubilized by Triton X-100 was measured in homogeneous and light-scattering media using the photosensitized inactivation of lysozyme as an internal actinometer. Higher values of phi delta at 630 nm than at 514 nm are attributed to the formation of a far-red-absorbing photosensitizing photoproduct. Topics: Azides; Darkness; Dose-Response Relationship, Radiation; Imidazoles; Kinetics; Light; Micrococcus luteus; Muramidase; Oxygen; Porphyrins; Scattering, Radiation; Singlet Oxygen; Superoxide Dismutase | 1994 |
INVESTIGATION OF THE ACTIVE SITES OF LYSOZYME. CARBOXYMETHYLATION OF THE IMIDAZOLE GROUP OF HISTIDINE AND OF THE EPSILON-AMINOGROUP OF LYSINE.
Topics: Alkylation; Catalytic Domain; Chromatography; Histidine; Imidazoles; Lysine; Methylation; Muramidase; Research; Spectrophotometry | 1964 |