pubmed-article:5881661 | rdf:type | pubmed:Citation | lld:pubmed |
pubmed-article:5881661 | lifeskim:mentions | umls-concept:C0043393 | lld:lifeskim |
pubmed-article:5881661 | lifeskim:mentions | umls-concept:C0020205 | lld:lifeskim |
pubmed-article:5881661 | lifeskim:mentions | umls-concept:C0178719 | lld:lifeskim |
pubmed-article:5881661 | lifeskim:mentions | umls-concept:C0040814 | lld:lifeskim |
pubmed-article:5881661 | pubmed:issue | 3 | lld:pubmed |
pubmed-article:5881661 | pubmed:dateCreated | 1966-7-24 | lld:pubmed |
pubmed-article:5881661 | pubmed:abstractText | 1. The trehalase found in an extract prepared from a yeast strain that cannot ferment trehalose was studied and characterized. The enzyme is highly specific for trehalose with K(m) 1.02x10(-2)m, and an optimum pH of 6.9. 2. It is inhibited by glucose and by trehalose 6-phosphate, and does not facilitate any significant transglucosylations. 3. pK values 7.7 and 5.8 were detected for the groups associated with binding of the non-ionized substrate to the enzyme. 4. The trehalase was found to be highly labile and was inhibited by thiol-binding reagents. 5. The possible role of this enzyme in the trehalose-dissimilation patterns in the yeast cell was evaluated. | lld:pubmed |
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pubmed-article:5881661 | pubmed:language | eng | lld:pubmed |
pubmed-article:5881661 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:5881661 | pubmed:citationSubset | IM | lld:pubmed |
pubmed-article:5881661 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
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pubmed-article:5881661 | pubmed:status | MEDLINE | lld:pubmed |
pubmed-article:5881661 | pubmed:month | Dec | lld:pubmed |
pubmed-article:5881661 | pubmed:issn | 0264-6021 | lld:pubmed |
pubmed-article:5881661 | pubmed:author | pubmed-author:AvigadGG | lld:pubmed |
pubmed-article:5881661 | pubmed:author | pubmed-author:NeufeldEE | lld:pubmed |
pubmed-article:5881661 | pubmed:author | pubmed-author:ZivOO | lld:pubmed |
pubmed-article:5881661 | pubmed:issnType | Print | lld:pubmed |
pubmed-article:5881661 | pubmed:volume | 97 | lld:pubmed |
pubmed-article:5881661 | pubmed:owner | NLM | lld:pubmed |
pubmed-article:5881661 | pubmed:authorsComplete | Y | lld:pubmed |
pubmed-article:5881661 | pubmed:pagination | 715-22 | lld:pubmed |
pubmed-article:5881661 | pubmed:dateRevised | 2009-11-18 | lld:pubmed |
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pubmed-article:5881661 | pubmed:year | 1965 | lld:pubmed |
pubmed-article:5881661 | pubmed:articleTitle | Intracellular trehalase of a hybrid yeast. | lld:pubmed |
pubmed-article:5881661 | pubmed:publicationType | Journal Article | lld:pubmed |
pubmed-article:5881661 | pubmed:publicationType | In Vitro | lld:pubmed |
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