Detail of "24967-27-9"

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Uremic peak 2a in high performance liquid chromatography

Uremic peak 2a in high performance liquid chromatography. Acidic components and their membrane permeability. Koide, Keizo; Toyama, Junko; Inoue, Noboru; Koshikawa, Shozo; Akizawa, Tadao; Takahashi, Ken; Hidaka, Saburo; Yamane, Yoshiji; Shinoda, Kiichi; et al. (Oji Natl. Hosp., Japan). Jpn. J. Nephrol., 28(11), 1481-9 (Japanese) 1986. CODEN: NJGKAU. ISSN: 0385-2385. DOCUMENT TYPE: Journal CA Section: 9 (Biochemical Methods) Section cross-reference(s): 14 Uremic peak 2a has previously been detected by HPLC of uremic fluids such as plasma and hemofiltrates (HF). The peak fraction from HF was further analyzed by anion-exchange HPLC to examine acidic components. At least eight main peaks were detected commonly among patients with chronic renal failure as acidic subfractions of 2a. Each peak was again fractionated and the main components were analyzed by UV spectra, NMR, and gas chromatog., resulting in detection of org. acids such as neuraminic acid deriv., N-phenylacetylglutamine, quinolinic acid, p-carboxyphenyl glucuronide, oxypruinol uronide, trans-acotinic acid, and 2,5-furandicarboxylic acid. Since the components were rather low mol. wt., membrane permeability of the peaks was examd. by using ultrafiltration membranes of different cut-off mol. wt., 500, 1000 and 5000. The peaks behaved as if their mol. wt. 108115-71-5 and 24967-27-9 which are cas registry numbers of substances are two of reagents here. were between 1000 and 5000 in spite of their components of rather low mol. wt. One of the reasons was attributed to binding with medium size mols. (MW: 1000-3000) which were presumed to co-exist in 2a fraction. Such phenomena may explain a part of an elusive nature of middle mol. toxins. .

Investigation of Neuraminidase-Substrate Recognition Using Molecular Dynamics and Free Energy Calculations

Investigation of Neuraminidase-Substrate Recognition Using Molecular Dynamics and Free Energy Calculations. Masukawa, Kevin M.In this study， 139110-80-8 and 24967-27-9 are also used.; Kollman, Peter A.; Kuntz, Irwin D. (Department of Pharmaceutical Chemistry, Chemistry and Chemical Biology Program, University of California San Francisco, San Francisco, CA 94143-2240, USA). Journal of Medicinal Chemistry, 46(26), 5628-5637 (English) 2003 American Chemical Society. CODEN: JMCMAR. ISSN: 0022-2623. DOCUMENT TYPE: Journal CA Section: 1 (Pharmacology) Development of the new generation of therapeutics against the influenza viral coat protein neuraminidase is a response to the continuing threat of influenza epidemics. A variety of structurally similar compds. have been reported that vary greatly in their ability to inhibit neuraminidase, a crit. enzyme that cleaves sialic acid and promotes virion release. To det. how neuraminidase exhibits this wide range of affinities with structurally similar compds., mol. dynamic simulations, coupled with free energy calcns., were used to det. the binding components of a series of neuraminidase inhibitors. Using four cocrystal structures of neuraminidase-inhibitor complexes, we examd. the structural and energetic components of ligand potency and selectivity. An in-depth energetic anal., including internal energy, entropy, and nonbonded interactions, reveals that potency of ligand binding is governed by nonpolar contacts. Electrostatic components generally oppose binding, although two of the best inhibitors use electrostatic interactions to orient the ligand. This investigation suggests that the enhanced selectivity and potency of the better ligands may arise from an improved positioning of their ligand atoms in the active site due to polar and hydrophobic functionalities. Simulations that included crystal water mols. in the active site indicate that the more potent ligands make less use of water-mediated interactions. .