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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
1
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pubmed:dateCreated |
1998-2-5
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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.
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pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Calcium,
http://linkedlifedata.com/resource/pubmed/chemical/Calcium-Binding Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Lactalbumin,
http://linkedlifedata.com/resource/pubmed/chemical/Muramidase,
http://linkedlifedata.com/resource/pubmed/chemical/Water
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pubmed:status |
MEDLINE
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pubmed:month |
Nov
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pubmed:issn |
0014-2956
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:day |
15
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pubmed:volume |
250
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
72-6
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pubmed:dateRevised |
2007-7-23
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pubmed:meshHeading |
pubmed-meshheading:9431992-Animals,
pubmed-meshheading:9431992-Binding Sites,
pubmed-meshheading:9431992-Calcium,
pubmed-meshheading:9431992-Calcium-Binding Proteins,
pubmed-meshheading:9431992-Cattle,
pubmed-meshheading:9431992-Egg White,
pubmed-meshheading:9431992-Horses,
pubmed-meshheading:9431992-Hydrogen Bonding,
pubmed-meshheading:9431992-Lactalbumin,
pubmed-meshheading:9431992-Muramidase,
pubmed-meshheading:9431992-Protein Binding,
pubmed-meshheading:9431992-Protein Conformation,
pubmed-meshheading:9431992-Spectrophotometry,
pubmed-meshheading:9431992-Spectroscopy, Fourier Transform Infrared,
pubmed-meshheading:9431992-Water
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pubmed:year |
1997
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pubmed:articleTitle |
Fourier-transform infrared spectroscopic studies on the coordination of the side-chain COO- groups to Ca2+ in equine lysozyme.
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pubmed:affiliation |
Division of Biological Sciences, Graduate School of Science, Hokkaido University, Sapporo, Japan.
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pubmed:publicationType |
Journal Article
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