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CTRB2 chymotrypsinogen B2

chymotrypsinogen A
Top mentioned proteins: Lysozyme, ACID, Chymotrypsin, CAN, Serum albumin
Papers on chymotrypsinogen A
One step physically adsorbed coating of silica capillary with excellent stability for the separation of basic proteins by capillary zone electrophoresis.
Zhang et al., Wuhan, China. In Talanta, Dec 2015
Using chitin coating, the adsorption of proteins on capillary inner surface was successfully suppressed with reversed and stable EOF, and four basic proteins including lysozyme, cytochrome c, ribonuclease A and α-chymotrypsinogen A were baseline separated within 16 min with satisfied separation efficiency using 20 mM pH 2.0 H3PO4-Na2HPO4 as back ground electrolyte and 20 kV as separation voltage.
A two level hierarchical model of protein retention in ion exchange chromatography.
Cavallotti et al., Milano, Italy. In J Chromatogr A, Oct 2015
Model predictions are tested against experimental data measured for Lysozyme and Chymotrypsinogen A in IEX columns as a function of ionic strength and pH.
Interactions of Multimodal Ligands with Proteins: Insights into Selectivity Using Molecular Dynamics Simulations.
Cramer et al., Troy, United States. In Langmuir, Aug 2015
Here we employ molecular dynamics (MD) simulations to investigate the interactions of three different proteins--ubiquitin, cytochrome C, and α-chymotrypsinogen A, sampling a range of charge from +1e to +9e--with two multimodal chromatographic ligands containing similar chemical moieties--aromatic, carboxyl, and amide--in different structural arrangements.
Displacement chromatography of proteins using a retained pH front in a hydrophobic charge induction chromatography column.
Frey et al., Baltimore, United States. In J Chromatogr A, Apr 2015
The separation of lysozyme and α-chymotrypsinogen A into adjoined, rectangular bands was accomplished with overall recoveries based on the total mass injected greater than 90 and 70%, respectively.
Cooperative Unfolding of Residual Structure in Heat Denatured Proteins by Urea and Guanidinium Chloride.
Ahmad et al., New Delhi, India. In Plos One, 2014
It is known that heat and guanidinium chloride (GdmCl) give structurally different states of RNase-A, lysozyme, α-chymotrypsinogen A and α-lactalbumin.
Interactions of urea with native and unfolded proteins: a volumetric study.
Chalikian et al., Toronto, Canada. In J Phys Chem B, 2014
We use this approach to analyze our urea-dependent data on the partial molar volume and adiabatic compressibility of lysozyme, apocytochrome c, ribonuclease A, and α-chymotrypsinogen A. The analysis produces the thermodynamic properties of elementary urea-protein association reactions while also yielding estimates of the effective solvent-accessible surface areas of the native and unfolded protein states.
Aggregates of α-chymotrypsinogen anneal to access more stable states.
Roberts et al., Newark, United States. In Biotechnol Bioeng, 2014
Here it is shown that under mildly-denaturing conditions (elevated temperature or [urea]), where the native monomer (N) is slightly favored compared to the unfolded state (U), α-chymotrypsinogen A (aCgn) non-native aggregates undergo a structural relaxation or annealing process to reach even more stable states.
Adsorption behavior of proteins on temperature-responsive resins.
Antos et al., Rzeszów, Poland. In J Chromatogr A, 2014
As model proteins lysozyme, lactoferrin, α-chymotrypsinogen A and ovalbumin have been used.
Reduction of the C191-C220 disulfide of α-chymotrypsinogen A reduces nucleation barriers for aggregation.
Roberts et al., Newark, United States. In Biophys Chem, 2014
Proper disulfide formation can be essential for the conformational stability of natively folded proteins.
Coarse-grained model for colloidal protein interactions, B(22), and protein cluster formation.
Roberts et al., Newark, United States. In J Phys Chem B, 2014
Model parametrization was done by fitting simulation results against experimental value of B22 as a function of solution ionic strength for α-chymotrypsinogen A and γD-Crystallin (gD-Crys).
N-methyl-2-pyrrolidonium methyl sulfonate acidic ionic liquid as a new dynamic coating for separation of basic proteins by capillary electrophoresis.
Zhang et al., Wuhan, China. In Electrophoresis, 2013
Consequently, under the optimum separation conditions, a satisfied separation of basic proteins including lysozyme, cytochrome c, ribonuclease A, and α-chymotrypsinogen A with theoretical plates ranging from 2.09 × 10(5) to 4.48 × 10(5) plates/m had been accomplished within 15 min.
Protein entrapment in PEGylated lipid nanoparticles.
Lesieur et al., Châtenay-Malabry, France. In Int J Pharm, 2013
Nanoencapsulation of three cationic proteins (human brain-derived neurotrophic factor (BDNF), α-chymotrypsinogen A, and histone H3) was investigated using anionic nanoparticle (NP) carriers.
Application of the copolymers containing sulfobetaine methacrylate in protein separation by capillary electrophoresis.
Wang et al., Hefei, China. In J Biomater Sci Polym Ed, 2012
Followed, the copolymer was applied to coat the fused-silica capillary inner wall, and the coated capillary was used to separate the mixture of proteins (lysozyme, cytochrome c, ribonuclease A, and α-chymotrypsinogen A) in a pH range from 3.0 to 5.0.
Selection of bovine catalase aptamers using non-SELEX.
Li et al., Singapore, Singapore. In Electrophoresis, 2012
lysozyme, trypsinogen, chymotrypsinogen A, and myoglobin) tested and this confirmed that the aptamer exhibited a distinct specificity toward bovine catalase.
Sulphydryl oxidase: oxidation of sulphydryl groups and the formation of three-dimensional structure in proteins.
Horton et al., In Ciba Found Symp, 1978
In the presence of sulphydryl oxidase, functional structure is rapidly acquired by both reductively unfolded ribonuclease A and reductively denatured immobilized chymotrypsinogen A as judged by restoration of native fluorescence characteristics and biological activity.
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