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Polyacetylene Compounds from Panax Ginseng C. A. Meyer
Shim, Sang-Chul,Koh, Hun-Yeoung,Han, Byung-Hoon Korean Chemical Society 1983 Bulletin of the Korean Chemical Society Vol.4 No.4
Two major and two minor polyacetylenes were isolated from fresh white Korean ginseng roots. The petroleum ether-ethyl ether fractions containing the polyacetylene compounds were collected through solvent fractionation, partition and silica gel column chromatography. Further separation of polyacetylenic fractions was proceeded by bonded normal phase HPLC utilizing a moderately nonpolar microparticulate column. The low pressure liquid chromatography was used for the semi-preparative separation. The chemical structures of the two major polyacetylenes separated were determined by UV, IR, $^1H$ NMR, $^{13}C$ NMR, mass spectra and elemental analysis. One of them is identified to be heptadeca-1-en-4, 6-diyne-3, 9, 10-triol, a new structure, and the other is heptadeca-1, 9-dien-4, 6-diyn-3-ol, known as panaxynol.
Kim, Wook-Hyun,Chung, Ji-Hyung,Back, Jung-Ho,Choi, Ju-Hyun,Cha, Joo-Hwan,Koh, Hun-Yeoung,Han, Ye-Sun Korean Society for Biochemistry and Molecular Biol 2003 Journal of biochemistry and molecular biology Vol.36 No.5
NAD(P)H quinone oxidoreductase is a ubiquitous enzyme that is known to directly reduce quinone substrates to hydroquinones by a two-electron reaction. We report the identification of NADPH quinone oxidoreductase from Kluyveromyces marxianus (KmQOR), which reduces quinone substrates directly to hydroquinones. The KmQOR gene was sequenced, expressed in Escherichia coli, purified, and characterized. The open-reading frame of the KmQOR gene consists of 1143 nucleotides, encoding a 380 amino acid polypeptide. The nucleotide sequence of the KmQOR gene was assigned to EMBL under accession number AY040868. The $M_r$ that was determined by SDS-PAGE for the protein subunit was about 42 kDa, and the molecular mass of the native KmQOR was 84 kDa, as determined by column calibration, indicating that the native protein is a homodimer. The KmQOR protein efficiently reduced 1,4-benzoquinone, whereas no activities were found for menadiones and methoxyquinones. These observations, and the result of an extended sequence analysis of known NADPH quinone oxidoreductase, suggest that KmQOR possesses a different action mechanism.
( Wook Hyun Kim ),( Ji Hyung Chung ),( Jung Ho Back ),( Ju Hyun Choi ),( Joo Hwan Cha ),( Hun Yeoung Koh ),( Ye Sun Han ) 생화학분자생물학회 2003 BMB Reports Vol.36 No.5
NAD(P)H quinone oxidoreductase is a ubiquitous enzyme that is known to directly reduce quinone substrates to hydroquinones by a two-electron reaction. We report the identification of NADPH quinone oxidoreductase from Kluyveromyces marxianus (KmQOR), which reduces quinone substrates directly to hydroquinones. The KmQOR gene was sequenced, expressed in Escherichia coli, purified, and characterized. The open-reading frame of the KmQOR gene consists of 1143 nucleotides, encoding a 380 amino acid polypeptide. The nucleotide sequence of the KmQOR gene was assigned to EMBL under accession number AT040868. The M, that was determined by SDS-PAGE for the protein subunit was about 42 kDa, and the molecular mass of the native KmQOR was 84 kDa, as determined by column calibration, indicating that the native protein is a homodimer. The KmQOR protein efficiently reduced 1,4-benzoquinone, whereas no activities were found for menadiones and methoxyquinones. These observations, and the result of an extended sequence analysis of known NADPH quinone oxidoreductase, suggest that KmQOR possesses a different action mechanism.