ABSTRACT
Rat globin peptides alkylated by sulfur mustard on amino-acid residues C-126, C-93 and E-27 with MH+ 1444.62 Da, 1561.66 Da, 1676.78 Da, respectively, were concentrated using metal-affinity chromatography on Cu2+. The peptides were received by trypic digestion after in vitro incubation of rat globin with 60 microM HD. Aklylated peptide with MH+ 1444.62 Da is the most sensitive biomarker, which can be concentrated from globin trypic digest, incubated with 3 microM sulfur mustard.
Subject(s)
Chromatography, Affinity/methods , Hemoglobins/chemistry , Hemoglobins/isolation & purification , Mustard Gas/chemistry , Alkylation , Animals , RatsABSTRACT
The possibility of interaction of 0.1 mg/mL acetylsalicylic acid with purified human and rat globin in vitro during 24 h at 37 degrees C was investigated. The rat globin can be modified with acetylsalicylic acid on aminoacid residues K-17, K-57, K-91, K-140 in alpha subunit as well as on K-18, K-77 in beta subunit. The human globin can be modified with acetylsalicylic acid on aminoacid residues K-17, K-41, K-57 and K-91 in alpha subunit as well as on K-18, K-96 and K- 133 in beta subunit. We identified of acetetylated lysines K-17 and K-57 in alpha subunit of human hemoglobin after incubation whole blood with 0.1 mg/mL acetylsalicylic acid during 3 h.
Subject(s)
Aspirin/chemistry , Hemoglobins/chemistry , Acetylation , Animals , Humans , Rats , Time FactorsABSTRACT
The physico-chemical characteristic of medicinal preparations used for the treatment of various bladder diseases is provided including their electrophoretic activity and the ability to penetrate into bladder tissues, e.g. during electrophoresis. The optimal parameters of intracavitary electrophoresis are considered.
Subject(s)
Anti-Infective Agents, Urinary/pharmacokinetics , Electrochemotherapy/methods , Urinary Bladder Diseases/drug therapy , Urinary Bladder/metabolism , Animals , Anti-Infective Agents, Urinary/pharmacology , Drug Evaluation , Humans , Swine , Urinary Bladder Diseases/metabolismABSTRACT
A possibility to improve the thermal properties of holographic gratings in a photosensitive system based on polymethylmethacrylate (PMMA) and to enhance simultaneously the adhesion of the photopolymer to soda-lime glass is demonstrated. The modified PMMA was prepared by radical copolymerisation of methylmethacrylate (MMA) with acrylic acid (AA). Polymer films deposited from samples of the copolymer of MMA with AA containing 9,10-phenanthrenequinone additives were used as a photosensitive material for the recording of holographic gratings. It is possible to generate gratings that are thermally stable up to 200 masculineC using this modified PMMA. Dynamic thermogravimetry, differential thermal analysis and thermal mechanic analyses were used to determine the dependence of the thermal stability of the modified PMMA on the composition and the structure of its macromolecules.
ABSTRACT
Interaction of ten different lipopolysaccharides (LPS) with 2,4-dinitrofluorobenzene yielded quantitatively yellow dinitrophenyl derivatives (DNP-LPS) to show the presence of substituents with free amino group. The DNP-LPS samples were degraded with 1% acetic acid, and after removal of lipid A precipitates the supernatants were separated on a Sephadex G-25 column to give coloured polysaccharide, oligosaccharide and monomeric fractions monitored at lambda DNP = 365 nm. The coloured materials, including DNP-derivative of lipid A, were dephosphorylated with hydrofluoric acid followed by identification of the released DNP-amines by thin layer chromatography (TLC) on silica gel. Subsequently, the dephosphorylated materials were hydrolysed with hydrochloric acid followed by TLC analysis. The approach allowed to detect, locate and identify the substituents with free amino group within the LPS molecules. Moreover, two types of core structures within LPS preparation from one strain were discovered for five microorganisms.
