Source:http://linkedlifedata.com/resource/pubmed/id/12907158
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| Predicate | Object |
|---|---|
| rdf:type | |
| lifeskim:mentions | |
| pubmed:issue |
3
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| pubmed:dateCreated |
2003-8-8
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| pubmed:abstractText |
Information about beta-crystallins and their post-translational modifications has been scarce because of difficulties in isolating the individual beta-crystallins. These difficulties arise because the beta-crystallin sequences are highly homologous and because beta-crystallins undergo many age-related modifications that lead to a variety of molecular masses and a range of acidities for each crystallin. In this study, human beta-crystallins were isolated using several steps of chromatography both before and after two-dimensional gel electrophoresis. Many previously unidentified in vivo modifications, including deamidations among all beta-crystallins except betaB3, truncation of betaA3, betaB1 and betaA4, and oxidation of some methionines and tryptophans were located among the isolated beta-crystallins. Many modifications occurred before age 20 with modest increases in modification for beta-crystallins from lenses 20-87 years old. The tendency of the modified beta-crystallins to form non-covalent complexes was evident from their chromatographic behaviour. The presence in these complexes of betaB2-crystallin, the least modified and most soluble of the beta-crystallins, points to a possible role for betaB2 in solubilizing the more heavily modified beta-crystallins. The greater solubility of beta-crystallins compared with alpha- and gamma-crystallins in aging lenses may be due to beta-crystallin modifications and their non-covalent associations.
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| pubmed:grant | |
| pubmed:language |
eng
|
| pubmed:journal | |
| pubmed:citationSubset |
IM
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| pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/CRYBA4 protein, human,
http://linkedlifedata.com/resource/pubmed/chemical/CRYBB1 protein, human,
http://linkedlifedata.com/resource/pubmed/chemical/CRYBB3 protein, human,
http://linkedlifedata.com/resource/pubmed/chemical/Crystallins,
http://linkedlifedata.com/resource/pubmed/chemical/Methionine,
http://linkedlifedata.com/resource/pubmed/chemical/Tryptophan,
http://linkedlifedata.com/resource/pubmed/chemical/beta-Crystallin A Chain,
http://linkedlifedata.com/resource/pubmed/chemical/beta-Crystallin B Chain,
http://linkedlifedata.com/resource/pubmed/chemical/beta-crystallin B2
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| pubmed:status |
MEDLINE
|
| pubmed:month |
Sep
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| pubmed:issn |
0014-4835
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| pubmed:author | |
| pubmed:issnType |
Print
|
| pubmed:volume |
77
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| pubmed:owner |
NLM
|
| pubmed:authorsComplete |
Y
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| pubmed:pagination |
259-72
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| pubmed:dateRevised |
2007-11-14
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| pubmed:meshHeading |
pubmed-meshheading:12907158-Adult,
pubmed-meshheading:12907158-Aged,
pubmed-meshheading:12907158-Aged, 80 and over,
pubmed-meshheading:12907158-Aging,
pubmed-meshheading:12907158-Child,
pubmed-meshheading:12907158-Child, Preschool,
pubmed-meshheading:12907158-Chromatography, High Pressure Liquid,
pubmed-meshheading:12907158-Crystallins,
pubmed-meshheading:12907158-Electrophoresis, Gel, Two-Dimensional,
pubmed-meshheading:12907158-Humans,
pubmed-meshheading:12907158-Lens, Crystalline,
pubmed-meshheading:12907158-Methionine,
pubmed-meshheading:12907158-Middle Aged,
pubmed-meshheading:12907158-Oxidation-Reduction,
pubmed-meshheading:12907158-Protein Biosynthesis,
pubmed-meshheading:12907158-Tryptophan,
pubmed-meshheading:12907158-beta-Crystallin A Chain,
pubmed-meshheading:12907158-beta-Crystallin B Chain
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| pubmed:year |
2003
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| pubmed:articleTitle |
Human beta-crystallins modified by backbone cleavage, deamidation and oxidation are prone to associate.
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| pubmed:affiliation |
Department of Chemistry, University of Nebraska, Lincoln, NE 68588-0304, USA.
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| pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.,
Research Support, Non-U.S. Gov't
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