| pubmed-article:6405788 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:6405788 | lifeskim:mentions | umls-concept:C0009630 | lld:lifeskim |
| pubmed-article:6405788 | lifeskim:mentions | umls-concept:C0022952 | lld:lifeskim |
| pubmed-article:6405788 | lifeskim:mentions | umls-concept:C0872079 | lld:lifeskim |
| pubmed-article:6405788 | lifeskim:mentions | umls-concept:C0185125 | lld:lifeskim |
| pubmed-article:6405788 | lifeskim:mentions | umls-concept:C0182400 | lld:lifeskim |
| pubmed-article:6405788 | lifeskim:mentions | umls-concept:C1524063 | lld:lifeskim |
| pubmed-article:6405788 | pubmed:issue | 1 | lld:pubmed |
| pubmed-article:6405788 | pubmed:dateCreated | 1983-7-15 | lld:pubmed |
| pubmed-article:6405788 | pubmed:abstractText | Galactosyltransferase (EC 2.4.1.38) has been shown to bind to Con A-Sepharose. Concentrations of methyl-alpha-mannoside greater than 0.7 M were required to release the enzyme from the immobilized lectin. Molecular weight determination by gel filtration revealed that galactosyltransferase formed a 1:1 complex with concanavalin A. Preincubation of the enzyme with excess concanavalin A did not affect its catalytic activity either in the presence or absence of alpha-lactalbumin. The galactosyltransferase-concanavalin A complex was retained on an alpha-lactalbumin-Sepharose column in the presence of N-acetylglucosamine and manganese chloride and was eluted from the column in their absence. Galactosyltransferase immobilized onto a Con A-Sepharose was still active either in the presence or absence of alpha-lactalbumin. Lactose synthase activity was also observed when the galactosyltransferase-concanavalin A complex was assayed with alpha-lactalbumin immobilized on Sepharose. These data indicate that the carbohydrate moiety of galactosyltransferase is involved in neither the catalytic process nor the binding of alpha-lactalbumin and must be linked to the enzyme at a location where it does not present any steric hindrance on the binding of concanavalin A, either free or immobilized on Sepharose. | lld:pubmed |
| pubmed-article:6405788 | pubmed:grant | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:6405788 | pubmed:language | eng | lld:pubmed |
| pubmed-article:6405788 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:6405788 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:6405788 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:6405788 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:6405788 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:6405788 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:6405788 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:6405788 | pubmed:month | May | lld:pubmed |
| pubmed-article:6405788 | pubmed:issn | 0006-3002 | lld:pubmed |
| pubmed-article:6405788 | pubmed:author | pubmed-author:ELYJ WJW | lld:pubmed |
| pubmed-article:6405788 | pubmed:author | pubmed-author:WongS SSS | lld:pubmed |
| pubmed-article:6405788 | pubmed:author | pubmed-author:MaloneT ETE | lld:pubmed |
| pubmed-article:6405788 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:6405788 | pubmed:day | 30 | lld:pubmed |
| pubmed-article:6405788 | pubmed:volume | 745 | lld:pubmed |
| pubmed-article:6405788 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:6405788 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:6405788 | pubmed:pagination | 90-6 | lld:pubmed |
| pubmed-article:6405788 | pubmed:dateRevised | 2007-11-14 | lld:pubmed |
| pubmed-article:6405788 | pubmed:meshHeading | pubmed-meshheading:6405788-... | lld:pubmed |
| pubmed-article:6405788 | pubmed:meshHeading | pubmed-meshheading:6405788-... | lld:pubmed |
| pubmed-article:6405788 | pubmed:meshHeading | pubmed-meshheading:6405788-... | lld:pubmed |
| pubmed-article:6405788 | pubmed:meshHeading | pubmed-meshheading:6405788-... | lld:pubmed |
| pubmed-article:6405788 | pubmed:meshHeading | pubmed-meshheading:6405788-... | lld:pubmed |
| pubmed-article:6405788 | pubmed:meshHeading | pubmed-meshheading:6405788-... | lld:pubmed |
| pubmed-article:6405788 | pubmed:meshHeading | pubmed-meshheading:6405788-... | lld:pubmed |
| pubmed-article:6405788 | pubmed:meshHeading | pubmed-meshheading:6405788-... | lld:pubmed |
| pubmed-article:6405788 | pubmed:meshHeading | pubmed-meshheading:6405788-... | lld:pubmed |
| pubmed-article:6405788 | pubmed:year | 1983 | lld:pubmed |
| pubmed-article:6405788 | pubmed:articleTitle | Use of concanavalin A as a topographical probe for protein-protein interaction. Application to lactose synthase. | lld:pubmed |
| pubmed-article:6405788 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:6405788 | pubmed:publicationType | Research Support, U.S. Gov't, P.H.S. | lld:pubmed |
