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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
2
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pubmed:dateCreated |
1986-3-12
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pubmed:abstractText |
The physicochemical properties of a novel Mr-21 000 Ca2+-binding protein isolated from bovine brain were investigated. The protein exhibited a partial specific volume of 0.724 ml/g, a degree of hydration of 0.47 g of water/g of protein and a mean residue weight of 119. Sedimentation equilibrium analysis revealed Mr = 22 600 in the absence of Ca2+; Ca2+ binding appeared to induce dimerization of the molecule. Size-exclusion chromatography indicated a compacting of the molecule on binding of Ca2+: the Stokes radius decreased from 2.75 nm in the absence of Ca2+ to 2.56 nm in its presence. Far-u.v.c.d. spectroscopy showed the apoprotein to be composed of 44% alpha-helix, 18% beta-pleated sheet and 38% random coil. Addition of either KCl (0.1 M) plus Mg2+ (1 mM), or Ca2+ (2 mM), changed the conformation to 49% alpha-helix, 18% beta-pleated sheet and 33% random coil. Near-u.v.c.d. and u.v. difference spectroscopy both indicated perturbations in the environments of all three types of aromatic amino acids on binding of Ca2+. Ca2+ binding also resulted in a 30% enhancement in the tryptophan fluorescence emission intensity. Ca2+ titration of the far-u.v.c.d. and fluorescence enhancement provided KD values of 9.91 microM and 4.68 microM respectively. Finally, the protein was shown to bind Zn2+ with KD = 1.44 microM (no Mg2+) and 1.82 microM (+ Mg2+). These observations strongly support the possibility that this novel Ca2+-binding protein resembles calmodulin and related Ca2+-binding proteins and undergoes a conformational change on binding of Ca2+ which reflects a physiological role in Ca2+-mediated regulation of brain function.
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pubmed:commentsCorrections |
http://linkedlifedata.com/resource/pubmed/commentcorrection/4091809-14663,
http://linkedlifedata.com/resource/pubmed/commentcorrection/4091809-193856,
http://linkedlifedata.com/resource/pubmed/commentcorrection/4091809-199586,
http://linkedlifedata.com/resource/pubmed/commentcorrection/4091809-200611,
http://linkedlifedata.com/resource/pubmed/commentcorrection/4091809-202300,
http://linkedlifedata.com/resource/pubmed/commentcorrection/4091809-4091808,
http://linkedlifedata.com/resource/pubmed/commentcorrection/4091809-4270462,
http://linkedlifedata.com/resource/pubmed/commentcorrection/4091809-436009,
http://linkedlifedata.com/resource/pubmed/commentcorrection/4091809-4366945,
http://linkedlifedata.com/resource/pubmed/commentcorrection/4091809-4598824,
http://linkedlifedata.com/resource/pubmed/commentcorrection/4091809-5045520,
http://linkedlifedata.com/resource/pubmed/commentcorrection/4091809-5329026,
http://linkedlifedata.com/resource/pubmed/commentcorrection/4091809-6095814,
http://linkedlifedata.com/resource/pubmed/commentcorrection/4091809-6105043,
http://linkedlifedata.com/resource/pubmed/commentcorrection/4091809-6201746,
http://linkedlifedata.com/resource/pubmed/commentcorrection/4091809-6213623,
http://linkedlifedata.com/resource/pubmed/commentcorrection/4091809-6236084,
http://linkedlifedata.com/resource/pubmed/commentcorrection/4091809-6243188,
http://linkedlifedata.com/resource/pubmed/commentcorrection/4091809-6250447,
http://linkedlifedata.com/resource/pubmed/commentcorrection/4091809-6250577,
http://linkedlifedata.com/resource/pubmed/commentcorrection/4091809-6254958,
http://linkedlifedata.com/resource/pubmed/commentcorrection/4091809-6275425,
http://linkedlifedata.com/resource/pubmed/commentcorrection/4091809-6316082,
http://linkedlifedata.com/resource/pubmed/commentcorrection/4091809-6351918,
http://linkedlifedata.com/resource/pubmed/commentcorrection/4091809-6615807,
http://linkedlifedata.com/resource/pubmed/commentcorrection/4091809-6799500,
http://linkedlifedata.com/resource/pubmed/commentcorrection/4091809-7074011,
http://linkedlifedata.com/resource/pubmed/commentcorrection/4091809-708687,
http://linkedlifedata.com/resource/pubmed/commentcorrection/4091809-7093208,
http://linkedlifedata.com/resource/pubmed/commentcorrection/4091809-7352978,
http://linkedlifedata.com/resource/pubmed/commentcorrection/4091809-7407067
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
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pubmed:status |
MEDLINE
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pubmed:month |
Dec
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pubmed:issn |
0264-6021
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:day |
1
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pubmed:volume |
232
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
569-75
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pubmed:dateRevised |
2009-11-18
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pubmed:meshHeading |
pubmed-meshheading:4091809-Animals,
pubmed-meshheading:4091809-Brain Chemistry,
pubmed-meshheading:4091809-Calcium-Binding Proteins,
pubmed-meshheading:4091809-Cations, Divalent,
pubmed-meshheading:4091809-Cattle,
pubmed-meshheading:4091809-Centrifugation, Density Gradient,
pubmed-meshheading:4091809-Circular Dichroism,
pubmed-meshheading:4091809-Molecular Weight,
pubmed-meshheading:4091809-Protein Conformation,
pubmed-meshheading:4091809-Spectrometry, Fluorescence,
pubmed-meshheading:4091809-Spectrophotometry, Ultraviolet
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pubmed:year |
1985
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pubmed:articleTitle |
Physicochemical properties of a novel Mr-21 000 Ca2+-binding protein of bovine brain.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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