Hypericum japonicum Thunb./Vincetoxicum officinale, Sedum caucasicum and other plant spp
2-(3,4-Dihydroxyphenyl)-3,5-dihydroxy-4-oxo-4H-chromen-7-yl 6-deoxy-α-L-mannopyranoside/4H-1-Benzopyran-4-one, 7-((6-deoxy-α-L-mannopyranosyl)oxy)-2-(3,4-dihydroxyphenyl)-3,5-dihydroxy-/4H-1-Benzopyran-4-one, 7-[(6-deoxy-α-L-mannopyranosyl)oxy]-2-(3,4-dihydroxyphenyl)-3,5-dihydroxy-/Quercetin-7-O-rhamnoside/2-(3,4-dihydroxyphenyl)-3,5-dihydroxy-7-[(2S,3R,4R,5R,6S)-3,4,5-trihydroxy-6-methyloxan-2-yl]oxychromen-4-one/7-Rhamnosylquercetin/quercetin 7-O-alpha-L-rhamnopyranoside/Vincetoxicoside B/Quercetin 7-rhamnoside
Chemical constituents from the rhizome of Polygonum paleaceum and their antifungal activity. PUMID/DOI：27309618 J Asian Nat Prod Res. 2017 Jan;19(1):47-52. A new compounds neopaleaceolactoside (1), along with nine known compounds phyllocoumarin (2), quercetin (3), quercitrin (4), quercetin-3-methyl ether (5), Vincetoxicoside B (6), isoquercitrin (7), kaempferol (8), (-)-epicatechin (9), and chlorogenic acid (10), was isolated from Polygonum paleaceum Wall. Their chemical structures were established based on one-dimensional and two-dimensional nuclear magnetic resonance techniques, mass spectrometry and by comparison with spectroscopic data reported. Some selected compounds were screened for their antifungal activity. Quercetin (3), Vincetoxicoside B (6), kaempferol (8), and (-)-epicatechin (9) showed synergistic antifungal activities with the FICI values <0.5. A preliminary structure-activity relationship could be observed that free 3-OH in the structure of flavonoids was important for synergistic antifungal activity.
801.1±65.0 °C at 760 mmHg
74-175℃ (methanol )
HS Code Reference
Personal Projective Equipment
For Reference Standard and R&D, Not for Human Use Directly.
provides coniferyl ferulate(CAS#:22007-72-3) MSDS, density, melting point, boiling point, structure, formula, molecular weight etc. Articles of coniferyl ferulate are included as well.>> amp version: coniferyl ferulate
1. Proteoglycan aggregates from bovine nasal cartilage were studied by using electron microscopy of proteoglycan/cytochrome c monolayers. 2. The aggregates contained a variably long central filament of hyaluronic acid with an average length of 1037nm. The proteoglycan monomers attached to the hyaluronic acid appeared as side chain filaments varying in length (averaging 249nm). They were distributed along the central filament at an average distance of about 36nm. 3. Chondroitin sulphate side chains were removed from the proteoglycan monomers of the aggregates by partial chondroitinase digestion. The molecules obtained had the same general appearance as intact aggregates. 4. Proteoglycan aggregates were treated with trypsin and the largest fragment, which contains the hyaluronic acid, link protein and hyaluronic acid-binding region, was recovered and studied with electron microscopy. Filaments that lacked the side chain extensions and had the same length as the central filament in the intact aggregate were observed. 5. Hyaluronic acid isolated after papain digestion of cartilage extracts gave filaments with similar length and size distribution as observed for the central filament both in the intact aggregate and in the trypsin digests. 6. Umbilical-cord hyaluronic acid was also studied and gave electron micrographs similar to those described for hyaluronic acid from cartilage. However, the length of the filament was somewhat shorter. 7. The electron micrographs of both intact and selectively degraded proteoglycans corroborate the current model of cartilage proteoglycan structure.
Cartilage proteoglycan aggregates. Electronmicroscopic studies of native and fragmented molecules
Dick Heinegard,* Stefan Lohmander,†‡ and Johan Thyberg†
1978 Dec 1;
Foetal human lung fibroblasts, grown in monolayer, were allowed to incorporate 35SO42− for various periods of time. 35S-labelled macromolecular anionic products were isolated from the medium, a trypsin digest of the cells in monolayer and the cell residue. The various radioactive polysaccharides were identified as heparan sulphate and a galactosaminoglycan population (chondroitin sulphate and dermatan sulphate) by ion-exchange chromatography and by differential degradations with HNO2 and chondroitinase ABC. Most of the heparan sulphate was found in the trypsin digest, whereas the galactosaminoglycan components were largely confined to the medium. Electrophoretic studies on the various 35S-labelled galactosaminoglycans suggested the presence of a separate chondroitin sulphate component (i.e. a glucuronic acid-rich galactosaminoglycan). The 35S-labelled galactosaminoglycans were subjected to periodate oxidation of l-iduronic acid residues followed by scission in alkali. A periodate-resistant polymer fraction was obtained, which could be degraded to disaccharides by chondroitinase AC. However, most of the 35S-labelled galactosaminoglycans were extensively degraded by periodate oxidation-alkaline elimination. The oligosaccharides obtained were essentially resistant to chondroitinase AC, indicating that the iduronic acid-rich galactosaminoglycans (i.e. dermatan sulphate) were composed largely of repeating units containing sulphated or non-sulphated l-iduronic acid residues. The l-iduronic acid residues present in dermatan sulphate derived from the medium and the trypsin digest contained twice as much ester sulphate as did material associated with the cells. The content of d-glucuronic acid was low and similar in all three fractions. The relative distribution of glycosaminoglycans among the various fractions obtained from cultured lung fibroblasts was distinctly different from that of skin fibroblasts [Malmstrom, Carlstedt, aberg & Fransson (1975) Biochem. J. 151, 477-489]. Moreover, subtle differences in co-polymeric structure of dermatan sulphate isolated from the two cell types could be detected.
Synthesis of glycosaminoglycans by human embryonic lung fibroblasts. Different distribution of heparan sulphate, chondroitin sulphate and dermatan sulphate in various fractions of the cell culture
Ingrid Sjoberg and Lars-ake Fransson
1977 Nov 1;
Several polyclonal sera were raised in rabbits and in mice against putative sucrose carrier proteins, i.e. a 42 kilodalton (O Gallet, R Lemoine, C Larsson, S Delrot  Biochim Biophys Acta 978: 56-64) and a 62 kD (KG Ripp, PV Viitanen, WD Hitz, VR Fransceschi  Plant Physiol 88: 1435-1445) polypeptide of the plasma membrane. The effects of these sera on the active uptake of sucrose and of valine into purified plasma membrane vesicles from sugar beet (Beta vulgaris L.) leaves and roots were studied. At a dilution of 1/50, the anti-42 kilodalton sera consistently inhibited sucrose uptake in plasma membranes from leaves or from roots. They had no effect on valine uptake. Under the same experimental conditions, the anti-62 kilodalton sera had no effect on active uptake of sucrose. The data further support the view that a 42 kilodalton polypeptide is a component of the transport system mediating sucrose uptake across the plasma membrane of plant cells.
Selective Inhibition of Active Uptake of Sucrose into Plasma Membrane Vesicles by Polyclonal Sera Directed against a 42 Kilodalton Plasma Membrane Polypeptide 1
Olivier Gallet, Remi Lemoine, Cecile Gaillard, Christer Larsson, and Serge Delrot