| pubmed-article:7228874 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:7228874 | lifeskim:mentions | umls-concept:C0001811 | lld:lifeskim |
| pubmed-article:7228874 | lifeskim:mentions | umls-concept:C0007452 | lld:lifeskim |
| pubmed-article:7228874 | lifeskim:mentions | umls-concept:C0023317 | lld:lifeskim |
| pubmed-article:7228874 | lifeskim:mentions | umls-concept:C0010422 | lld:lifeskim |
| pubmed-article:7228874 | lifeskim:mentions | umls-concept:C1280500 | lld:lifeskim |
| pubmed-article:7228874 | lifeskim:mentions | umls-concept:C0598528 | lld:lifeskim |
| pubmed-article:7228874 | pubmed:issue | 10 | lld:pubmed |
| pubmed-article:7228874 | pubmed:dateCreated | 1981-7-20 | lld:pubmed |
| pubmed-article:7228874 | 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. | lld:pubmed |
| pubmed-article:7228874 | pubmed:grant | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:7228874 | pubmed:grant | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:7228874 | pubmed:language | eng | lld:pubmed |
| pubmed-article:7228874 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:7228874 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:7228874 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:7228874 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:7228874 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:7228874 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:7228874 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:7228874 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:7228874 | pubmed:month | May | lld:pubmed |
| pubmed-article:7228874 | pubmed:issn | 0021-9258 | lld:pubmed |
| pubmed-article:7228874 | pubmed:author | pubmed-author:ChylackL... | lld:pubmed |
| pubmed-article:7228874 | pubmed:author | pubmed-author:BunnH FHF | lld:pubmed |
| pubmed-article:7228874 | pubmed:author | pubmed-author:RabyCC | lld:pubmed |
| pubmed-article:7228874 | pubmed:author | pubmed-author:ChiouS HSH | lld:pubmed |
| pubmed-article:7228874 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:7228874 | pubmed:day | 25 | lld:pubmed |
| pubmed-article:7228874 | pubmed:volume | 256 | lld:pubmed |
| pubmed-article:7228874 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:7228874 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:7228874 | pubmed:pagination | 5176-80 | lld:pubmed |
| pubmed-article:7228874 | pubmed:dateRevised | 2007-11-14 | lld:pubmed |
| pubmed-article:7228874 | pubmed:meshHeading | pubmed-meshheading:7228874-... | lld:pubmed |
| pubmed-article:7228874 | pubmed:meshHeading | pubmed-meshheading:7228874-... | lld:pubmed |
| pubmed-article:7228874 | pubmed:meshHeading | pubmed-meshheading:7228874-... | lld:pubmed |
| pubmed-article:7228874 | pubmed:meshHeading | pubmed-meshheading:7228874-... | lld:pubmed |
| pubmed-article:7228874 | pubmed:meshHeading | pubmed-meshheading:7228874-... | lld:pubmed |
| pubmed-article:7228874 | pubmed:meshHeading | pubmed-meshheading:7228874-... | lld:pubmed |
| pubmed-article:7228874 | pubmed:meshHeading | pubmed-meshheading:7228874-... | lld:pubmed |
| pubmed-article:7228874 | pubmed:meshHeading | pubmed-meshheading:7228874-... | lld:pubmed |
| pubmed-article:7228874 | pubmed:meshHeading | pubmed-meshheading:7228874-... | lld:pubmed |
| pubmed-article:7228874 | pubmed:meshHeading | pubmed-meshheading:7228874-... | lld:pubmed |
| pubmed-article:7228874 | pubmed:meshHeading | pubmed-meshheading:7228874-... | lld:pubmed |
| pubmed-article:7228874 | pubmed:year | 1981 | lld:pubmed |
| pubmed-article:7228874 | pubmed:articleTitle | Nonenzymatic glycosylation of bovine lens crystallins. Effect of aging. | lld:pubmed |
| pubmed-article:7228874 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:7228874 | pubmed:publicationType | Research Support, U.S. Gov't, P.H.S. | lld:pubmed |
| pubmed-article:7228874 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:7228874 | lld:pubmed |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:7228874 | lld:pubmed |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:7228874 | lld:pubmed |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:7228874 | lld:pubmed |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:7228874 | lld:pubmed |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:7228874 | lld:pubmed |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:7228874 | lld:pubmed |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:7228874 | lld:pubmed |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:7228874 | lld:pubmed |
