| pubmed-article:2674939 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:2674939 | lifeskim:mentions | umls-concept:C0086418 | lld:lifeskim |
| pubmed-article:2674939 | lifeskim:mentions | umls-concept:C0026794 | lld:lifeskim |
| pubmed-article:2674939 | lifeskim:mentions | umls-concept:C0005456 | lld:lifeskim |
| pubmed-article:2674939 | lifeskim:mentions | umls-concept:C0205360 | lld:lifeskim |
| pubmed-article:2674939 | lifeskim:mentions | umls-concept:C0596235 | lld:lifeskim |
| pubmed-article:2674939 | lifeskim:mentions | umls-concept:C0678594 | lld:lifeskim |
| pubmed-article:2674939 | lifeskim:mentions | umls-concept:C1706214 | lld:lifeskim |
| pubmed-article:2674939 | lifeskim:mentions | umls-concept:C1707689 | lld:lifeskim |
| pubmed-article:2674939 | lifeskim:mentions | umls-concept:C2349975 | lld:lifeskim |
| pubmed-article:2674939 | pubmed:issue | 18 | lld:pubmed |
| pubmed-article:2674939 | pubmed:dateCreated | 1989-10-24 | lld:pubmed |
| pubmed-article:2674939 | pubmed:abstractText | A Ca2+ binding site like an EF-hand motif was designed and created in human lysozyme by replacing both Gln-86 and Ala-92 with aspartic acids by site-directed mutagenesis. The mutant human lysozyme (D86/92-lysozyme) was expressed and secreted by yeast. One Ca2+ was found to bind one molecule of the purified protein with the binding constant 5.0 x 10(6) M-1. The enzymatic activity of holo-D86/92-lysozyme against glycol chitin at 40 degrees C was 2-fold higher than that of the native lysozyme. Maximal activity of the holo-D86/92-lysozyme was observed at 80 degrees C, where its relative activity normalized to the value at 40 degrees C was 6-fold and 17-fold higher than those of the native and apoenzymes, respectively. The activities of the native lysozyme and apo-D86/92-lysozyme were maximum at 65 degrees C-70 degrees C. Moreover, D86/92-lysozyme was more stable against protease digestion than the native lysozyme. These results indicate that the creation of the calcium binding site like an EF-hand motif in the human lysozyme enhances its structural stability. | lld:pubmed |
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| pubmed-article:2674939 | pubmed:language | eng | lld:pubmed |
| pubmed-article:2674939 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:2674939 | pubmed:citationSubset | IM | lld:pubmed |
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| pubmed-article:2674939 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:2674939 | pubmed:month | Sep | lld:pubmed |
| pubmed-article:2674939 | pubmed:issn | 0027-8424 | lld:pubmed |
| pubmed-article:2674939 | pubmed:author | pubmed-author:NakamuraHH | lld:pubmed |
| pubmed-article:2674939 | pubmed:author | pubmed-author:IkeharaMM | lld:pubmed |
| pubmed-article:2674939 | pubmed:author | pubmed-author:KikuchiMM | lld:pubmed |
| pubmed-article:2674939 | pubmed:author | pubmed-author:TaniyamaYY | lld:pubmed |
| pubmed-article:2674939 | pubmed:author | pubmed-author:KurokiRR | lld:pubmed |
| pubmed-article:2674939 | pubmed:author | pubmed-author:SekiEE | lld:pubmed |
| pubmed-article:2674939 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:2674939 | pubmed:volume | 86 | lld:pubmed |
| pubmed-article:2674939 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:2674939 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:2674939 | pubmed:pagination | 6903-7 | lld:pubmed |
| pubmed-article:2674939 | pubmed:dateRevised | 2009-11-18 | lld:pubmed |
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| pubmed-article:2674939 | pubmed:year | 1989 | lld:pubmed |
| pubmed-article:2674939 | pubmed:articleTitle | Design and creation of a Ca2+ binding site in human lysozyme to enhance structural stability. | lld:pubmed |
| pubmed-article:2674939 | pubmed:affiliation | Protein Engineering Research Institute, Osaka, Japan. | lld:pubmed |
| pubmed-article:2674939 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:2674939 | pubmed:publicationType | Comparative Study | lld:pubmed |
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