muramidase has been researched along with triethylamine* in 3 studies
3 other study(ies) available for muramidase and triethylamine
| Article | Year |
|---|---|
Optimization of the capillary zone electrophoresis loading limit and resolution of proteins, using triethylamine, ammonium formate and acidic pH.
Capillary zone electrophoresis (CZE) of five model proteins (lysozyme, myoglobin, ribonuclease A, alpha-lactalbumin, and trypsinogen), using ammonium formate as the electrophoretic buffer and triethylamine (TEA) as a buffer additive at pH 2.5, was used for protein separation. The electrophoretic behavior of these proteins was examined with respect to various concentrations (10-40 mM) of TEA and of ammonium formate. Based on the experimental parameters of electrophoretic resolution, current, and peak separation time, an electrolyte (30 mM each of TEA and ammonium formate) was empirically derived as the optimum for scale-up separation. The loading limit for proteins, covering a wide range of injection volumes (60-990 nl) and amount of protein (1-21 pmol of each protein), was investigated on 75 and 100 microns I.D. untreated fused-silica capillaries. Protein adsorption (average < 15%) was experimentally determined using this volatile buffer system. Topics: Adsorption; Animals; Buffers; Cattle; Chickens; Electrophoresis, Capillary; Ethylamines; Formates; Horses; Hydrogen-Ion Concentration; Indicators and Reagents; Isoelectric Point; Lactalbumin; Molecular Weight; Muramidase; Myoglobin; Proteins; Ribonuclease, Pancreatic; Trypsinogen | 1997 |
Amino acid analysis by HPLC: optimized conditions for chromatography of phenylthiocarbamyl derivatives.
A method for analysis of phenylthiocarbamyl-amino acids by HPLC is described. Solvent A contains 0.05 M sodium acetate plus triethylamine (2.75 ml/liter) adjusted to pH 6.40 with phosphoric acid. Solvent B consists of 50% solvent A, 40% acetonitrile, and 10% methanol. The stationary phase is a 3-micron Spherisorb ODS-2 column (4.6 X 100 mm). A new sample can be injected every 27 min. Variation of the triethylamine concentration from 1 to 4 ml/liter is shown to affect column selectivity in a predictable manner, and this provides a rational basis for optimizing chromatographic conditions. Resolution of certain hydrophilic amino acids (Arg, Thr, Ala, and Pro), and mobile phase stability are improved over previously described procedures. Topics: Amino Acids; Autoanalysis; Chromatography, High Pressure Liquid; Egg White; Ethylamines; Fibrinopeptide A; Isothiocyanates; Muramidase; Thiocyanates | 1986 |
Obviation of destructive action of 0.2 M NaOH on proteins during arginine modification with cyclohexanedione by use of 0.1 M triethylamine as solvent.
The use of 0.2 M NaOH as a solvent for modification of arginine residues by 1,2-cyclohexanedione in disulfide containing proteins is destructive to the disulfide bonds. Modification can be conveniently done in 0.1 M triethylamine (pH 10.9) without any deleterious effect. Lysozyme was found to retain all its enzymic activity in 0.1 M triethylamine (pH 10.9) whereas complete loss of activity took place in 0.2 M NaOH. Topics: Arginine; Cyclohexanones; Disulfides; Ethylamines; Humans; Hydrogen-Ion Concentration; Immunoglobulin G; Indicators and Reagents; Kinetics; Lactalbumin; Muramidase; Proteins; Serum Albumin, Bovine; Sodium Hydroxide; Solvents | 1971 |