| pubmed-article:2914853 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:2914853 | lifeskim:mentions | umls-concept:C0004587 | lld:lifeskim |
| pubmed-article:2914853 | lifeskim:mentions | umls-concept:C0080194 | lld:lifeskim |
| pubmed-article:2914853 | lifeskim:mentions | umls-concept:C0017982 | lld:lifeskim |
| pubmed-article:2914853 | lifeskim:mentions | umls-concept:C0678594 | lld:lifeskim |
| pubmed-article:2914853 | lifeskim:mentions | umls-concept:C0065067 | lld:lifeskim |
| pubmed-article:2914853 | pubmed:issue | 1 | lld:pubmed |
| pubmed-article:2914853 | pubmed:dateCreated | 1989-3-13 | lld:pubmed |
| pubmed-article:2914853 | pubmed:abstractText | The occurrence, structure, and glycosylation of lipoteichoic acids were studied in 15 Bacillus strains, including Bacillus cereus (4 strains), Bacillus subtilis (5 strains), Bacillus licheniformis (1 strain), Bacillus polymyxa (2 strains), and Bacillus circulans (3 strains). Whereas in the cells of B. polymyxa and B. circulans neither lipoteichoic acid nor related amphipathic polymer could be detected, the cells of other Bacillus strains were shown to contain lipoteichoic acids built up of poly(glycerol phosphate) backbone chains and hydrophobic anchors [gentiobiosyl(beta 1----1/3)diacylglycerol or monoacylglycerol]. The lipoteichoic acid chains of the B. licheniformis strain and three of the B. subtilis strains had N-acetylglucosamine side branches, but those of the B. cereus strains and the remaining two B. subtilis strains did not. The membranes of the B. licheniformis strain and the first three B. subtilis strains exhibited enzyme activities for the synthesis of beta-N-acetylglucosamine-P-polyprenol and for the transfer of N-acetylglucosamine from this glycolipid to endogenous acceptors presumed to be lipoteichoic acid precursors. In contrast, the membranes of the other strains lacked both or either of these two enzyme activities. The correlation between the occurrence of N-acetylglucosamine-linked lipoteichoic acids and the distribution of these enzymes is consistent with the previously proposed function of beta-N-acetylglucosamine-P-polyprenol as a glycosyl donor in the introduction of alpha-N-acetylglucosamine branches to lipoteichoic acid backbone chains. | lld:pubmed |
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| pubmed-article:2914853 | pubmed:language | eng | lld:pubmed |
| pubmed-article:2914853 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:2914853 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:2914853 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
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| pubmed-article:2914853 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:2914853 | pubmed:month | Jan | lld:pubmed |
| pubmed-article:2914853 | pubmed:issn | 0021-9193 | lld:pubmed |
| pubmed-article:2914853 | pubmed:author | pubmed-author:ItoEE | lld:pubmed |
| pubmed-article:2914853 | pubmed:author | pubmed-author:IwasakiHH | lld:pubmed |
| pubmed-article:2914853 | pubmed:author | pubmed-author:ShimadaAA | lld:pubmed |
| pubmed-article:2914853 | pubmed:author | pubmed-author:YokoyamaKK | lld:pubmed |
| pubmed-article:2914853 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:2914853 | pubmed:volume | 171 | lld:pubmed |
| pubmed-article:2914853 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:2914853 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:2914853 | pubmed:pagination | 424-9 | lld:pubmed |
| pubmed-article:2914853 | pubmed:dateRevised | 2009-11-18 | lld:pubmed |
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| pubmed-article:2914853 | pubmed:meshHeading | pubmed-meshheading:2914853-... | lld:pubmed |
| pubmed-article:2914853 | pubmed:year | 1989 | lld:pubmed |
| pubmed-article:2914853 | pubmed:articleTitle | Structure and glycosylation of lipoteichoic acids in Bacillus strains. | lld:pubmed |
| pubmed-article:2914853 | pubmed:affiliation | Department of Chemistry, Faculty of Science, Hokkaido University, Sapporo, Japan. | lld:pubmed |
| pubmed-article:2914853 | pubmed:publicationType | Journal Article | lld:pubmed |
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