| pubmed-article:10680170 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:10680170 | lifeskim:mentions | umls-concept:C0007634 | lld:lifeskim |
| pubmed-article:10680170 | lifeskim:mentions | umls-concept:C0034727 | lld:lifeskim |
| pubmed-article:10680170 | lifeskim:mentions | umls-concept:C0020306 | lld:lifeskim |
| pubmed-article:10680170 | lifeskim:mentions | umls-concept:C0002518 | lld:lifeskim |
| pubmed-article:10680170 | lifeskim:mentions | umls-concept:C0728938 | lld:lifeskim |
| pubmed-article:10680170 | pubmed:issue | 2 | lld:pubmed |
| pubmed-article:10680170 | pubmed:dateCreated | 2000-3-15 | lld:pubmed |
| pubmed-article:10680170 | pubmed:abstractText | Plant cell suspension cultures of Rauvolfia are able to produce a high amount of arbutin by glucosylation of exogenously added hydroquinone. A four step purification procedure using anion exchange, hydrophobic interaction, hydroxyapatite-chromatography and chromatofocusing delivered in a yield of 0.5%, an approximately 390 fold enrichment of the involved glucosyltransferase. SDS-PAGE showed a M(r) for the enzyme of 52 kDa. Proteolysis of the pure enzyme with endoproteinase LysC revealed six peptide fragments with 9-23 amino acids which were sequenced. Sequence alignment of the six peptides showed high homologies to glycosyltransferases from other higher plants. | lld:pubmed |
| pubmed-article:10680170 | pubmed:language | eng | lld:pubmed |
| pubmed-article:10680170 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:10680170 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:10680170 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:10680170 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:10680170 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:10680170 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:10680170 | pubmed:month | Jan | lld:pubmed |
| pubmed-article:10680170 | pubmed:issn | 0031-9422 | lld:pubmed |
| pubmed-article:10680170 | pubmed:author | pubmed-author:StöckigtJJ | lld:pubmed |
| pubmed-article:10680170 | pubmed:author | pubmed-author:ArenaGG | lld:pubmed |
| pubmed-article:10680170 | pubmed:author | pubmed-author:WarzechaHH | lld:pubmed |
| pubmed-article:10680170 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:10680170 | pubmed:volume | 53 | lld:pubmed |
| pubmed-article:10680170 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:10680170 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:10680170 | pubmed:pagination | 187-93 | lld:pubmed |
| pubmed-article:10680170 | pubmed:dateRevised | 2006-11-15 | lld:pubmed |
| pubmed-article:10680170 | pubmed:meshHeading | pubmed-meshheading:10680170... | lld:pubmed |
| pubmed-article:10680170 | pubmed:meshHeading | pubmed-meshheading:10680170... | lld:pubmed |
| pubmed-article:10680170 | pubmed:meshHeading | pubmed-meshheading:10680170... | lld:pubmed |
| pubmed-article:10680170 | pubmed:meshHeading | pubmed-meshheading:10680170... | lld:pubmed |
| pubmed-article:10680170 | pubmed:meshHeading | pubmed-meshheading:10680170... | lld:pubmed |
| pubmed-article:10680170 | pubmed:meshHeading | pubmed-meshheading:10680170... | lld:pubmed |
| pubmed-article:10680170 | pubmed:meshHeading | pubmed-meshheading:10680170... | lld:pubmed |
| pubmed-article:10680170 | pubmed:meshHeading | pubmed-meshheading:10680170... | lld:pubmed |
| pubmed-article:10680170 | pubmed:meshHeading | pubmed-meshheading:10680170... | lld:pubmed |
| pubmed-article:10680170 | pubmed:meshHeading | pubmed-meshheading:10680170... | lld:pubmed |
| pubmed-article:10680170 | pubmed:meshHeading | pubmed-meshheading:10680170... | lld:pubmed |
| pubmed-article:10680170 | pubmed:meshHeading | pubmed-meshheading:10680170... | lld:pubmed |
| pubmed-article:10680170 | pubmed:meshHeading | pubmed-meshheading:10680170... | lld:pubmed |
| pubmed-article:10680170 | pubmed:year | 2000 | lld:pubmed |
| pubmed-article:10680170 | pubmed:articleTitle | Hydroquinone: O-glucosyltransferase from cultivated Rauvolfia cells: enrichment and partial amino acid sequences. | lld:pubmed |
| pubmed-article:10680170 | pubmed:affiliation | Department of Pharmaceutical Biology, Johannes Gutenberg-University, Mainz, Germany. | lld:pubmed |
| pubmed-article:10680170 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:10680170 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
