Switch to
| Predicate | Object |
|---|---|
| rdf:type | |
| lifeskim:mentions | |
| pubmed:issue |
5
|
| pubmed:dateCreated |
1998-5-26
|
| pubmed:abstractText |
The aim of the current study is to detect glycation of betaL-, betaS- and gamma-crystallins in the young bovine lens. To determine which of the crystallins are glycated, we have made isoelectric focusing of the water-soluble crystallins of four bovine lenses of 1. 183+/-0.070 years. Samples are stained: (1) with Coomassie Brilliant Blue for proteins; (2) with the lectin Concanavalin-A, followed by horse-radish peroxidase (HRP) and diaminobenzidine (DAB). Experiments are performed with crystallins in native form, in absence of denaturants. The crystallins are separated by isoelectric focusing into: alpha-crystallins of high-molecular weight (HM)-, alphaL-, betaH-, betaL-, betaS- and gamma-crystallins. In the lectin staining experiments only HM-, beta L-, betaS- and gamma-crystallins are positive, whereas the alphaL- and betaH-crystallins do not stain. Though glycation in the bovine lens is very low, lectin staining is sufficiently sensitive to detect the various glycated crystallins.
|
| pubmed:language |
eng
|
| pubmed:journal | |
| pubmed:citationSubset |
IM
|
| pubmed:chemical | |
| pubmed:status |
MEDLINE
|
| pubmed:month |
Nov
|
| pubmed:issn |
0014-4835
|
| pubmed:author | |
| pubmed:copyrightInfo |
Copyright 1997 Academic Press Limited.
|
| pubmed:issnType |
Print
|
| pubmed:volume |
65
|
| pubmed:owner |
NLM
|
| pubmed:authorsComplete |
Y
|
| pubmed:pagination |
711-5
|
| pubmed:dateRevised |
2003-11-14
|
| pubmed:meshHeading | |
| pubmed:year |
1997
|
| pubmed:articleTitle |
The glycation of bovine lens betaL-, betaS- and gamma-crystallins demonstrated by isoelectric focusing and lectin staining.
|
| pubmed:affiliation |
Institute of Experimental Ophthalmology, University of Bonn, Bonn, D-53105, Germany.
|
| pubmed:publicationType |
Journal Article
|