| pubmed-article:5054461 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:5054461 | lifeskim:mentions | umls-concept:C0086418 | lld:lifeskim |
| pubmed-article:5054461 | lifeskim:mentions | umls-concept:C0229671 | lld:lifeskim |
| pubmed-article:5054461 | lifeskim:mentions | umls-concept:C0005767 | lld:lifeskim |
| pubmed-article:5054461 | lifeskim:mentions | umls-concept:C0014780 | lld:lifeskim |
| pubmed-article:5054461 | lifeskim:mentions | umls-concept:C0016964 | lld:lifeskim |
| pubmed-article:5054461 | lifeskim:mentions | umls-concept:C0085249 | lld:lifeskim |
| pubmed-article:5054461 | lifeskim:mentions | umls-concept:C0702242 | lld:lifeskim |
| pubmed-article:5054461 | pubmed:issue | 8 | lld:pubmed |
| pubmed-article:5054461 | pubmed:dateCreated | 1972-10-18 | lld:pubmed |
| pubmed-article:5054461 | pubmed:abstractText | Human serum and hemoglobin-free erythrocyte membranes were found to contain a galactosyltransferase which catalyzes the transfer of galactose from UDP-galactose to specific large and small molecular weight acceptors. The requirements for enzyme activity were found to be similar for the enzymes from both sources. However, the membrane-bound enzyme depended on a detergent for maximal activity. Mn(++) was an absolute requirement for transfer and uridine nucleoside phosphates were inhibitors. The most effective acceptor for galactose was a glycoprotein containing N-acetylglucosamine residues in the terminal position of its oligosaccharide side chains, N-acetylglucosamine was also an acceptor. While the presence of alpha-lactalbumin in the incubation medium resulted in a significant decrease in the transfer of galactose to N-acetylglucosamine, glucose, which was not an acceptor for galactose in the absence of alpha-lactalbumin, became an excellent acceptor. The serum enzyme catalyzed the transfer of 54 nmoles of galactose per milliliter of serum per hour and its apparent K(m) for UDP-galactose was 7.5 x 10(-6)M. The membrane enzyme had a similar apparent K(m). Using a quantitative assay system the enzyme was found to be present in all individuals studied, regardless of their blood type, secretor status, or sex. | lld:pubmed |
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| pubmed-article:5054461 | pubmed:language | eng | lld:pubmed |
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| pubmed-article:5054461 | pubmed:citationSubset | AIM | lld:pubmed |
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| pubmed-article:5054461 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:5054461 | pubmed:month | Aug | lld:pubmed |
| pubmed-article:5054461 | pubmed:issn | 0021-9738 | lld:pubmed |
| pubmed-article:5054461 | pubmed:author | pubmed-author:KimY SYS | lld:pubmed |
| pubmed-article:5054461 | pubmed:author | pubmed-author:PerdomoJJ | lld:pubmed |
| pubmed-article:5054461 | pubmed:author | pubmed-author:WhiteheadJ... | lld:pubmed |
| pubmed-article:5054461 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:5054461 | pubmed:volume | 51 | lld:pubmed |
| pubmed-article:5054461 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:5054461 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:5054461 | pubmed:pagination | 2024-32 | lld:pubmed |
| pubmed-article:5054461 | pubmed:dateRevised | 2009-11-18 | lld:pubmed |
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| pubmed-article:5054461 | pubmed:year | 1972 | lld:pubmed |
| pubmed-article:5054461 | pubmed:articleTitle | Glycosyltransferases in human blood.I. Galactosyltransferase in human serum and erythrocyte membranes. | lld:pubmed |
| pubmed-article:5054461 | pubmed:publicationType | Journal Article | lld:pubmed |
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