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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
18
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pubmed:dateCreated |
1992-6-18
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pubmed:abstractText |
We have examined the molecular structure of the related neurotrophic factors brain-derived neurotrophic factor (BDNF) and neurotrophin-3 (NT-3) by physical methods, including gel filtration, velocity sedimentation, sedimentation equilibrium, urea gel electrophoresis, fluorescence spectroscopy, and far-ultraviolet circular dichroism. The results of these studies indicate that at physiologically relevant concentrations both recombinant proteins exist as tightly associated dimers. The dimers are stable even in 8 M solutions of urea. In solutions of guanidine hydrochloride, BDNF and NT-3 undergo slow unfolding between 3 and 5 M concentration of denaturant. Circular dichroism spectroscopy revealed approximately 70% beta-sheet and 20% beta-turn content in the native structure of both neurotrophic factors. In this respect, BDNF and NT-3 resemble other polypeptide growth factors whose receptors are also integral protein-tyrosine kinases.
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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 |
May
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pubmed:issn |
0006-2960
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:day |
12
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pubmed:volume |
31
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
4431-6
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pubmed:dateRevised |
2008-11-21
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pubmed:meshHeading |
pubmed-meshheading:1581298-Animals,
pubmed-meshheading:1581298-Brain Chemistry,
pubmed-meshheading:1581298-Brain-Derived Neurotrophic Factor,
pubmed-meshheading:1581298-CHO Cells,
pubmed-meshheading:1581298-Centrifugation, Density Gradient,
pubmed-meshheading:1581298-Chromatography, Gel,
pubmed-meshheading:1581298-Circular Dichroism,
pubmed-meshheading:1581298-Cricetinae,
pubmed-meshheading:1581298-Electrophoresis,
pubmed-meshheading:1581298-Hot Temperature,
pubmed-meshheading:1581298-Humans,
pubmed-meshheading:1581298-Mice,
pubmed-meshheading:1581298-Nerve Growth Factors,
pubmed-meshheading:1581298-Nerve Tissue Proteins,
pubmed-meshheading:1581298-Neurotrophin 3,
pubmed-meshheading:1581298-Protein Conformation,
pubmed-meshheading:1581298-Protein Denaturation,
pubmed-meshheading:1581298-Spectrometry, Fluorescence,
pubmed-meshheading:1581298-Structure-Activity Relationship
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pubmed:year |
1992
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pubmed:articleTitle |
Dimeric structure and conformational stability of brain-derived neurotrophic factor and neurotrophin-3.
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pubmed:affiliation |
Regeneron Pharmaceuticals Inc., Tarrytown, New York 10591.
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pubmed:publicationType |
Journal Article,
Comparative Study
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