| pubmed-article:1482181 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:1482181 | lifeskim:mentions | umls-concept:C0314926 | lld:lifeskim |
| pubmed-article:1482181 | lifeskim:mentions | umls-concept:C0007641 | lld:lifeskim |
| pubmed-article:1482181 | lifeskim:mentions | umls-concept:C2348043 | lld:lifeskim |
| pubmed-article:1482181 | lifeskim:mentions | umls-concept:C0871161 | lld:lifeskim |
| pubmed-article:1482181 | pubmed:issue | 11 | lld:pubmed |
| pubmed-article:1482181 | pubmed:dateCreated | 1993-2-10 | lld:pubmed |
| pubmed-article:1482181 | pubmed:abstractText | A pUC19-derived plasmid was constructed that coded for a hybrid cellulase with the Thermomonospora fusca E2 cellulose-binding domain at its C terminus joined to the Prevotella ruminicola 40.5-kDa carboxymethyl cellulase (CMCase). The hybrid enzyme was purified and characterized enzymatically. It bound tightly to cellulose, and its specific activities on carboxymethyl cellulose, amorphous cellulose, and ball-milled cellulose were 1.5, 10, and 8 times that of the 40.5-kDa CMCase, respectively. Furthermore, the modified enzyme gave synergism with an exocellulase in the degradation of filter paper, while the 40.5-kDa CMCase did not. | lld:pubmed |
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| pubmed-article:1482181 | pubmed:language | eng | lld:pubmed |
| pubmed-article:1482181 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:1482181 | pubmed:citationSubset | IM | lld:pubmed |
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| pubmed-article:1482181 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:1482181 | pubmed:month | Nov | lld:pubmed |
| pubmed-article:1482181 | pubmed:issn | 0099-2240 | lld:pubmed |
| pubmed-article:1482181 | pubmed:author | pubmed-author:WilsonD BDB | lld:pubmed |
| pubmed-article:1482181 | pubmed:author | pubmed-author:RussellJ BJB | lld:pubmed |
| pubmed-article:1482181 | pubmed:author | pubmed-author:MatsushitaOO | lld:pubmed |
| pubmed-article:1482181 | pubmed:author | pubmed-author:MaglioneGG | lld:pubmed |
| pubmed-article:1482181 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:1482181 | pubmed:volume | 58 | lld:pubmed |
| pubmed-article:1482181 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:1482181 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:1482181 | pubmed:pagination | 3593-7 | lld:pubmed |
| pubmed-article:1482181 | pubmed:dateRevised | 2010-11-18 | lld:pubmed |
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| pubmed-article:1482181 | pubmed:meshHeading | pubmed-meshheading:1482181-... | lld:pubmed |
| pubmed-article:1482181 | pubmed:year | 1992 | lld:pubmed |
| pubmed-article:1482181 | pubmed:articleTitle | Properties of a genetically reconstructed Prevotella ruminicola endoglucanase. | lld:pubmed |
| pubmed-article:1482181 | pubmed:affiliation | Section of Biochemistry, Molecular and Cell Biology, Cornell University, Ithaca, New York. | lld:pubmed |
| pubmed-article:1482181 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:1482181 | pubmed:publicationType | Research Support, U.S. Gov't, Non-P.H.S. | lld:pubmed |
| pubmed-article:1482181 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
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