Lipoxygenase inhibiting ethyl substituted glycoside from Symplocos racemosa.
Phytochemical investigation of Symplocos racemosa resulted in the isolation of a new ethyl substituted glycoside, 1-ethyl brachiose-3'-acetate ( 1 ) along with four known compounds ketochaulmoogric acid ( 2 ), nonaeicosanol ( 3 ), triacontyl palmitate ( 4 ) and methyl triacontanoate ( 5 ). The subst...
| Publicado en: | Natural Product Research Vol. 19; no. 5; pp. 509 - 516 |
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| Autores principales: | , , , , , , |
| Formato: | Journal Article |
| Publicado: |
Taylor & Francis Ltd
Jul2005
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| Acceso en línea: | Ver este registro en EBSCOhost |
| fields | @attributes: recordID: 1 pdfLink: plink: https://search.ebscohost.com/login.aspx?direct=true&db=ccm&AN=17000282&site=ehost-live header: @attributes: shortDbName: ccm uiTerm: 17000282 longDbName: CINAHL Complete uiTag: AN controlInfo: bkinfo: dissinfo: jinfo: jid: 14786419 RFT jtl: Natural Product Research issn: 14786419 maglogo: Y pubinfo: dt: Jul2005 vid: 19 iid: 5 pid: 377 pub: Taylor & Francis Ltd place: Philadelphia, Pennsylvania artinfo: ui: 17000282 10.1080/1478641042000261978 17000282 ppf: 509 ppct: 7 formats: tig: atl: Lipoxygenase inhibiting ethyl substituted glycoside from Symplocos racemosa. aug: au: Abbasi †, Muhammad Athar Ahmad, Viqar Uddin Zubair, Muhammad Nawaz, Sarfraz A. Lodhi, Muhammad Arif Farooq, Umar Choudhary, M. Iqbal sug: ab: Phytochemical investigation of Symplocos racemosa resulted in the isolation of a new ethyl substituted glycoside, 1-ethyl brachiose-3'-acetate ( 1 ) along with four known compounds ketochaulmoogric acid ( 2 ), nonaeicosanol ( 3 ), triacontyl palmitate ( 4 ) and methyl triacontanoate ( 5 ). The substitution of ethyl group on 1 was natural because during the course of extraction and purification ethanol was not used. The structural elucidation of the isolated compounds was based primarily on 1D- and 2D-NMR analysis, including COSY, HMQC, and HMBC correlations. The glycoside 1 and triacontyl palmitate ( 4 ) displayed the inhibitory potential against lipoxygenase and urease enzyme, respectively. pubtype: Academic Journal doctype: Journal Article ougenre: Article language: English refInfo: holdings: @attributes: islocal: N |
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