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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
2
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pubmed:dateCreated |
1984-5-11
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pubmed:abstractText |
The fluorescence parameters of demetallized alpha-lactalbumin in the range from pH 8 to 2 show an extreme around pH 5-4 (a minimum in quantum yield and wavelength and a maximum in polarization). This extreme is not due to a competition between Ca2+ and protons but rather to a stabilization of the conformation of the protein near the isoelectric pH by the ionic interactions between local positive and negative charges on the protein. The calcium-free protein has similar fluorescence characteristics at pH 2 and 8 but the thermal transition curve is different. The influence of 0.1 M NaCl is also considered.
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pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical | |
pubmed:status |
MEDLINE
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pubmed:month |
Mar
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pubmed:issn |
0006-291X
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:day |
15
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pubmed:volume |
119
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
509-15
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pubmed:dateRevised |
2003-11-14
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pubmed:meshHeading |
pubmed-meshheading:6712641-Animals,
pubmed-meshheading:6712641-Calcium,
pubmed-meshheading:6712641-Cattle,
pubmed-meshheading:6712641-Hydrogen-Ion Concentration,
pubmed-meshheading:6712641-Kinetics,
pubmed-meshheading:6712641-Lactalbumin,
pubmed-meshheading:6712641-Spectrometry, Fluorescence,
pubmed-meshheading:6712641-Temperature
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pubmed:year |
1984
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pubmed:articleTitle |
pH-dependence of the alpha-lactalbumin structure: a fluorescence study.
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pubmed:publicationType |
Journal Article
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