Linked Life Data

9702176

Source:http://linkedlifedata.com/resource/pubmed/id/9702176

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
1
pubmed:dateCreated
1998-9-11
pubmed:abstractText
The purpose of this study was to identify the major protein components in adult human lenses and to analyse the specific age-related changes in these proteins using two-dimensional electrophoresis, Edman sequencing, and in conjunction with the data in the accompanying manuscript, mass spectrometry. The majority of changes in the two-dimensional electrophoretic pattern of lens proteins occurred prior to 17 years of age, and included a decrease in proteins migrating to the original positions of beta B1, beta B3, beta A3, gamma C and gamma D, and the appearance of many new species with apparent molecular weights on two-dimensional electrophoretic gels similar to beta B2 and gamma S, but having more acidic pIs. These proteins were identified as deamidated forms of beta B1 and beta A3/A1 missing portions of their N-terminal extensions. With the exception of alpha B, deamidation was detected in all crystallin species. These data indicated that a major fraction of the water-soluble protein of the adult human lens is composed of truncated beta B1 and beta A3/A1 crystallins, and that nearly all human crystallins, including the, beta-crystallins, are susceptible to deamidation. The results also provided the most detailed map to date of the identities of protein species on two-dimensional electrophoresis gels of adult human lenses.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Jul
pubmed:issn
0014-4835
pubmed:author
pubmed:issnType
Print
pubmed:volume
67
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
31-43
pubmed:dateRevised
2007-11-14
pubmed:meshHeading
pubmed:year
1998
pubmed:articleTitle
Age-related changes in human lens crystallins identified by two-dimensional electrophoresis and mass spectrometry.
pubmed:affiliation
Department of Oral Molecular Biology, Oregon Health Sciences University, Portland 97201, USA.
pubmed:publicationType
Journal Article, Comparative Study, Research Support, U.S. Gov't, P.H.S.