Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:dateCreated
1989-2-7
pubmed:abstractText
Cation-exchange high-performance liquid chromatography on SynChropak CM300 in Tris-acetate buffers of pH 5-7, using sodium acetate gradients, produces an excellent separation of the various gamma-crystallin gene products and their post-synthetically modified forms from eye lens. With a single analysis of total lens extract, the gamma-crystallins can be resolved, quantified and collected for amino acid analysis. Experimental conditions are presented for optimal resolution of individual human, rat, bovine and dogfish shark gamma-crystallins. Applications presented include determinations of different synthesis of gamma-crystallins and chemical modification (oxidation by hydrogen peroxide) in situ.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Jul
pubmed:issn
0021-9673
pubmed:author
pubmed:issnType
Print
pubmed:day
1
pubmed:volume
444
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
239-50
pubmed:dateRevised
2007-11-14
pubmed:meshHeading
pubmed:year
1988
pubmed:articleTitle
Optimal resolution of eye lens gamma-crystallins by cation-exchange high-performance liquid chromatography on SynChropak CM300.
pubmed:affiliation
Department of Physics, Massachusetts Institute of Technology, Cambridge 02139.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S., Research Support, Non-U.S. Gov't