| pubmed-article:9431992 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:9431992 | lifeskim:mentions | umls-concept:C0441833 | lld:lifeskim |
| pubmed-article:9431992 | lifeskim:mentions | umls-concept:C0019944 | lld:lifeskim |
| pubmed-article:9431992 | lifeskim:mentions | umls-concept:C0026794 | lld:lifeskim |
| pubmed-article:9431992 | lifeskim:mentions | umls-concept:C0054739 | lld:lifeskim |
| pubmed-article:9431992 | lifeskim:mentions | umls-concept:C0596235 | lld:lifeskim |
| pubmed-article:9431992 | lifeskim:mentions | umls-concept:C2603343 | lld:lifeskim |
| pubmed-article:9431992 | lifeskim:mentions | umls-concept:C0242414 | lld:lifeskim |
| pubmed-article:9431992 | pubmed:issue | 1 | lld:pubmed |
| pubmed-article:9431992 | pubmed:dateCreated | 1998-2-5 | lld:pubmed |
| pubmed-article:9431992 | pubmed:abstractText | Interactions between Ca2+ and the Asp side chains in the Ca2+-binding site of equine lysozyme were investigated by Fourier-transform infrared (FT-IR) spectroscopy. In the spectrum of equine lysozyme, the intensities of the bands at about 1595 cm-1 and 1578 cm-1 in the region of the COO antisymmetric stretches increased upon Ca2+ binding. In the region of the COO- symmetric stretches, the loss of intensity at about 1388 cm-1 and gains of intensities at about 1423 cm-1 and 1403 cm-1 were observed due to Ca2+ binding to equine lysozyme. The spectral changes for equine lysozyme indicate that the COO- groups of Asp85, Asp90 and Asp91 in the Ca2+-binding site coordinate to Ca2+ in the pseudo-bridging mode, where divalent metal cation is bound to one of the two oxygens in the COO- group and a water molecule is hydrogen bonded to the other oxygen. The results presented here provide further evidence for a high degree of similarity between Ca2+-binding lysozyme and alpha-lactalbumin. The effects of Ca2+ binding on the main-chain conformation of equine lysozyme were compared with those of bovine alpha-lactalbumin and hen egg-white lysozyme. | lld:pubmed |
| pubmed-article:9431992 | pubmed:language | eng | lld:pubmed |
| pubmed-article:9431992 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:9431992 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:9431992 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:9431992 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:9431992 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:9431992 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:9431992 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:9431992 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:9431992 | pubmed:month | Nov | lld:pubmed |
| pubmed-article:9431992 | pubmed:issn | 0014-2956 | lld:pubmed |
| pubmed-article:9431992 | pubmed:author | pubmed-author:NittaKK | lld:pubmed |
| pubmed-article:9431992 | pubmed:author | pubmed-author:KawanoKK | lld:pubmed |
| pubmed-article:9431992 | pubmed:author | pubmed-author:NaraMM | lld:pubmed |
| pubmed-article:9431992 | pubmed:author | pubmed-author:MizuguchiMM | lld:pubmed |
| pubmed-article:9431992 | pubmed:author | pubmed-author:JuHH | lld:pubmed |
| pubmed-article:9431992 | pubmed:author | pubmed-author:HiraokiTT | lld:pubmed |
| pubmed-article:9431992 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:9431992 | pubmed:day | 15 | lld:pubmed |
| pubmed-article:9431992 | pubmed:volume | 250 | lld:pubmed |
| pubmed-article:9431992 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:9431992 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:9431992 | pubmed:pagination | 72-6 | lld:pubmed |
| pubmed-article:9431992 | pubmed:dateRevised | 2007-7-23 | lld:pubmed |
| pubmed-article:9431992 | pubmed:meshHeading | pubmed-meshheading:9431992-... | lld:pubmed |
| pubmed-article:9431992 | pubmed:meshHeading | pubmed-meshheading:9431992-... | lld:pubmed |
| pubmed-article:9431992 | pubmed:meshHeading | pubmed-meshheading:9431992-... | lld:pubmed |
| pubmed-article:9431992 | pubmed:meshHeading | pubmed-meshheading:9431992-... | lld:pubmed |
| pubmed-article:9431992 | pubmed:meshHeading | pubmed-meshheading:9431992-... | lld:pubmed |
| pubmed-article:9431992 | pubmed:meshHeading | pubmed-meshheading:9431992-... | lld:pubmed |
| pubmed-article:9431992 | pubmed:meshHeading | pubmed-meshheading:9431992-... | lld:pubmed |
| pubmed-article:9431992 | pubmed:meshHeading | pubmed-meshheading:9431992-... | lld:pubmed |
| pubmed-article:9431992 | pubmed:meshHeading | pubmed-meshheading:9431992-... | lld:pubmed |
| pubmed-article:9431992 | pubmed:meshHeading | pubmed-meshheading:9431992-... | lld:pubmed |
| pubmed-article:9431992 | pubmed:meshHeading | pubmed-meshheading:9431992-... | lld:pubmed |
| pubmed-article:9431992 | pubmed:meshHeading | pubmed-meshheading:9431992-... | lld:pubmed |
| pubmed-article:9431992 | pubmed:meshHeading | pubmed-meshheading:9431992-... | lld:pubmed |
| pubmed-article:9431992 | pubmed:meshHeading | pubmed-meshheading:9431992-... | lld:pubmed |
| pubmed-article:9431992 | pubmed:meshHeading | pubmed-meshheading:9431992-... | lld:pubmed |
| pubmed-article:9431992 | pubmed:year | 1997 | lld:pubmed |
| pubmed-article:9431992 | pubmed:articleTitle | Fourier-transform infrared spectroscopic studies on the coordination of the side-chain COO- groups to Ca2+ in equine lysozyme. | lld:pubmed |
| pubmed-article:9431992 | pubmed:affiliation | Division of Biological Sciences, Graduate School of Science, Hokkaido University, Sapporo, Japan. | lld:pubmed |
| pubmed-article:9431992 | pubmed:publicationType | Journal Article | lld:pubmed |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:9431992 | lld:pubmed |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:9431992 | lld:pubmed |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:9431992 | lld:pubmed |
