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| Predicate | Object |
|---|---|
| rdf:type | |
| lifeskim:mentions | |
| pubmed:issue |
5
|
| pubmed:dateCreated |
1984-7-27
|
| pubmed:abstractText |
Water-soluble (WS) and water-insoluble (WI) crystallins were prepared from calf and bovine lenses. The WS-crystallins were analyzed by capillary isotachophoresis and by immunoelectrophoresis with polyvalent and alpha-, beta-, gamma-crystallin specific antisera. The WI-crystallins were first solubilized in formamide and then analyzed by the same methods. The WS-crystallins, which increase in weight, but decrease in % with increasing age, show an increase of alpha-crystallins from 36 to 43%, an increase of beta-crystallins from 42 to 48% and a decrease of gamma-crystallins from 22 to 9%. In the WI-crystallins, which increase in weight and in % with increasing age, the alpha-crystallins form the main portion with an increase from 54 to 61%. The beta-crystallins in WI remain fairly constant at about 37% and the gamma-crystallins decrease from 8 to 2%. Quantitatively, the alpha-crystallin is the major constituent of the lens. The alpha-crystallin and the beta-crystallin components are increasingly incorporated in WI with increasing age. The gamma-crystallin components are selectively incorporated into WI-protein. Immunologically, alpha-, beta- and gamma-crystallins were detected by the polyvalent and specific antisera in WS- and in WI- crystallins.
|
| pubmed:language |
eng
|
| pubmed:journal | |
| pubmed:citationSubset |
IM
|
| pubmed:chemical | |
| pubmed:status |
MEDLINE
|
| pubmed:month |
May
|
| pubmed:issn |
0271-3683
|
| pubmed:author | |
| pubmed:issnType |
Print
|
| pubmed:volume |
3
|
| pubmed:owner |
NLM
|
| pubmed:authorsComplete |
Y
|
| pubmed:pagination |
691-7
|
| pubmed:dateRevised |
2006-11-15
|
| pubmed:meshHeading | |
| pubmed:year |
1984
|
| pubmed:articleTitle |
Isotachophoresis and immunoelectrophoresis of water-soluble and -insoluble crystallins of the ageing bovine lens.
|
| pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
|