| pubmed-article:3546309 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:3546309 | lifeskim:mentions | umls-concept:C0007004 | lld:lifeskim |
| pubmed-article:3546309 | lifeskim:mentions | umls-concept:C0439148 | lld:lifeskim |
| pubmed-article:3546309 | lifeskim:mentions | umls-concept:C0205369 | lld:lifeskim |
| pubmed-article:3546309 | lifeskim:mentions | umls-concept:C1998793 | lld:lifeskim |
| pubmed-article:3546309 | lifeskim:mentions | umls-concept:C0871161 | lld:lifeskim |
| pubmed-article:3546309 | lifeskim:mentions | umls-concept:C0059113 | lld:lifeskim |
| pubmed-article:3546309 | pubmed:issue | 8 | lld:pubmed |
| pubmed-article:3546309 | pubmed:dateCreated | 1987-4-20 | lld:pubmed |
| pubmed-article:3546309 | pubmed:abstractText | The soluble form of a bacteriophage-induced endo-N-acetylneuraminidase (Endo-N) specific for hydrolyzing oligo- or poly-alpha-2,8-linked sialosyl units in sources as disparate as bacterial and neural membrane glycoconjugates was purified approximately 10,000-fold and characterized. The enzyme appears homogenous by sodium dodecyl sulfate-polyacrylamide gel electrophoresis and has a subunit Mr 105,000. This corresponds to one of the higher Mr phage proteins which comprises 7.5% (by weight) of the total phage protein. The holoenzyme is active at neutral pH and has a Mr by gel filtration of 328,000, suggesting that the active enzyme is a trimer. Endo-N requires a minimum of 5 sialyl residues (DP5, where DP represents degree of polymerization) for activity. The limit digest products from the alpha-2,8-linked polysialic acid capsule of Escherichia coli K1 are DP4 with some DP3 and DP1,2. DP2-4 do not appear to inhibit depolymerization of polysialic acid. Endo-N digestion of the polysialosyl moiety on neural cell adhesion molecules yields sialyl oligomers with DP3 and DP4. The presence of a terminal sialitol changes both the distribution of limit digestion products and the apparent minimum substrate size. Higher Mr alpha-2,8-linked sialyl polymers (approximately DP200) are better substrates (Km 50-70 microM) than sialyl oligomers of approximately DP10-20 (Km 1.2 mM). Endo-N activity is inhibited by DNA and several other poly-anions tested. An examination of the distribution of intermediate products shows that Endo-N binds and cleaves at random sites on the polysialosyl chains, in contrast to initiating cleavage at one end and depolymerizing processively. Endo-N can serve as a specific molecular probe to detect and selectively modify poly-alpha-2,8-sialosyl carbohydrate units which have been implicated in bacterial meningitis and neural cell adhesion. | lld:pubmed |
| pubmed-article:3546309 | pubmed:grant | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:3546309 | pubmed:language | eng | lld:pubmed |
| pubmed-article:3546309 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:3546309 | pubmed:citationSubset | IM | lld:pubmed |
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| pubmed-article:3546309 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:3546309 | pubmed:month | Mar | lld:pubmed |
| pubmed-article:3546309 | pubmed:issn | 0021-9258 | lld:pubmed |
| pubmed-article:3546309 | pubmed:author | pubmed-author:TillM MMM | lld:pubmed |
| pubmed-article:3546309 | pubmed:author | pubmed-author:HallenbeckP... | lld:pubmed |
| pubmed-article:3546309 | pubmed:author | pubmed-author:REYR JRJ | lld:pubmed |
| pubmed-article:3546309 | pubmed:author | pubmed-author:VimrE RER | lld:pubmed |
| pubmed-article:3546309 | pubmed:author | pubmed-author:BasslerBB | lld:pubmed |
| pubmed-article:3546309 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:3546309 | pubmed:day | 15 | lld:pubmed |
| pubmed-article:3546309 | pubmed:volume | 262 | lld:pubmed |
| pubmed-article:3546309 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:3546309 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:3546309 | pubmed:pagination | 3553-61 | lld:pubmed |
| pubmed-article:3546309 | pubmed:dateRevised | 2007-11-14 | lld:pubmed |
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| pubmed-article:3546309 | pubmed:meshHeading | pubmed-meshheading:3546309-... | lld:pubmed |
| pubmed-article:3546309 | pubmed:year | 1987 | lld:pubmed |
| pubmed-article:3546309 | pubmed:articleTitle | Purification and properties of a bacteriophage-induced endo-N-acetylneuraminidase specific for poly-alpha-2,8-sialosyl carbohydrate units. | lld:pubmed |
| pubmed-article:3546309 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:3546309 | pubmed:publicationType | Research Support, U.S. Gov't, P.H.S. | lld:pubmed |
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