pubmed-article:6088322 | rdf:type | pubmed:Citation | lld:pubmed |
pubmed-article:6088322 | lifeskim:mentions | umls-concept:C0007452 | lld:lifeskim |
pubmed-article:6088322 | lifeskim:mentions | umls-concept:C0026131 | lld:lifeskim |
pubmed-article:6088322 | lifeskim:mentions | umls-concept:C0022952 | lld:lifeskim |
pubmed-article:6088322 | lifeskim:mentions | umls-concept:C0038734 | lld:lifeskim |
pubmed-article:6088322 | pubmed:issue | 8 | lld:pubmed |
pubmed-article:6088322 | pubmed:dateCreated | 1984-10-19 | lld:pubmed |
pubmed-article:6088322 | pubmed:abstractText | Galactosyltransferase from bovine milk was inactivated by a series of sulfhydryl group specific reagents of different structures and sizes. The inactivation rate constants suggest that the thiol is located in a nonpolar microenvironment. The ESR spectrum of a spin labeled galactosyltransferase showed that the sulfhydryl group is in a region of non-restricted rotation, consistent with its broad reactivity towards various thiol reagents. Galactosyltransferase immobilized onto agarose through its sulfhydryl group retained its ability to catalyze the synthesis of N-acetyllactosamine and lactose. Thus the residual activity of the sulfhydryl group modified enzyme is not due to an isozyme lacking such a group. In addition, the active thiol can not be located at the active site nor the protein-protein interaction site between galactosyltransferase and alpha-lactalbumin. | lld:pubmed |
pubmed-article:6088322 | pubmed:grant | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:6088322 | pubmed:language | eng | lld:pubmed |
pubmed-article:6088322 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:6088322 | pubmed:citationSubset | IM | lld:pubmed |
pubmed-article:6088322 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:6088322 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:6088322 | pubmed:status | MEDLINE | lld:pubmed |
pubmed-article:6088322 | pubmed:issn | 0020-711X | lld:pubmed |
pubmed-article:6088322 | pubmed:author | pubmed-author:WongS SSS | lld:pubmed |
pubmed-article:6088322 | pubmed:author | pubmed-author:WongL JLJ | lld:pubmed |
pubmed-article:6088322 | pubmed:issnType | Print | lld:pubmed |
pubmed-article:6088322 | pubmed:volume | 16 | lld:pubmed |
pubmed-article:6088322 | pubmed:owner | NLM | lld:pubmed |
pubmed-article:6088322 | pubmed:authorsComplete | Y | lld:pubmed |
pubmed-article:6088322 | pubmed:pagination | 913-7 | lld:pubmed |
pubmed-article:6088322 | pubmed:dateRevised | 2007-11-14 | lld:pubmed |
pubmed-article:6088322 | pubmed:meshHeading | pubmed-meshheading:6088322-... | lld:pubmed |
pubmed-article:6088322 | pubmed:meshHeading | pubmed-meshheading:6088322-... | lld:pubmed |
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pubmed-article:6088322 | pubmed:meshHeading | pubmed-meshheading:6088322-... | lld:pubmed |
pubmed-article:6088322 | pubmed:meshHeading | pubmed-meshheading:6088322-... | lld:pubmed |
pubmed-article:6088322 | pubmed:meshHeading | pubmed-meshheading:6088322-... | lld:pubmed |
pubmed-article:6088322 | pubmed:meshHeading | pubmed-meshheading:6088322-... | lld:pubmed |
pubmed-article:6088322 | pubmed:meshHeading | pubmed-meshheading:6088322-... | lld:pubmed |
pubmed-article:6088322 | pubmed:year | 1984 | lld:pubmed |
pubmed-article:6088322 | pubmed:articleTitle | The sulfhydryl group microenvironment of lactose synthase from bovine milk. | lld:pubmed |
pubmed-article:6088322 | pubmed:publicationType | Journal Article | lld:pubmed |
pubmed-article:6088322 | pubmed:publicationType | Research Support, U.S. Gov't, P.H.S. | lld:pubmed |
http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:6088322 | lld:pubmed |