Linked Life Data

7228874

Source:http://linkedlifedata.com/resource/pubmed/id/7228874

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
10
pubmed:dateCreated
1981-7-20
pubmed:abstractText
We have investigated nonenzymatic glycosylation of crystallins from calf and mature bovine lenses (2-6 years old). The lens homogenates were treated with 200-fold molar excess of [3H]NaBH4 and the incorporation of radioactivity was determined. The extent of glycosylation was more precisely determined from the 6 N HCl hydrolysate of [3H]borohydride-treated proteins by analyzing the glucitol-lysine adduct on a high pressure cation exchange column. We found that the [3H]NaBH4 incorporation and the amount of glucitol-lysine detected increased with age, particularly in HM alpha crystallin, a high molecular weight aggregate which accumulates with aging. This age-related increase in nonenzymatic glycosylation was also demonstrated by a comparison of crystallins isolated from the cortex and nucleus of a single lens. Nonenzymatic glycosylation of lens crystallins exemplifies a new form of post-transitional modification of long-lived proteins in vivo.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
May
pubmed:issn
0021-9258
pubmed:author
pubmed:issnType
Print
pubmed:day
25
pubmed:volume
256
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
5176-80
pubmed:dateRevised
2007-11-14
pubmed:meshHeading
pubmed:year
1981
pubmed:articleTitle
Nonenzymatic glycosylation of bovine lens crystallins. Effect of aging.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S., Research Support, Non-U.S. Gov't