Linked Life Data

3259558

Source:http://linkedlifedata.com/resource/pubmed/id/3259558

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
3
pubmed:dateCreated
1988-6-28
pubmed:abstractText
gamma-Crystallins were isolated from the homogenate of frog eye lenses (Rana catesbeiana) by exclusion gel chromatography and further purified by cation-exchange chromatography. They were the only group of crystallins possessing free amino groups amenable to sequence analysis by Edman degradation. Comparison of the amino acid contents of the purified subfractions of gamma-crystallins indicated their close relatedness in amino acid compositions and probably sequence homology as well. The amino-terminal sequence analysis of the purified gamma-crystallin subfractions showed extensive homology between these amphibian gamma-crystallin polypeptides themselves and also those from other vertebrate species, suggesting the existence of a multigene family and their close relatedness to gamma-crystallins of other vertebrates. The sequence comparison of the gamma-crystallin polypeptides from all major classes of vertebrates has provided strong support for the divergent evolution of gamma-crystallin family.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Mar
pubmed:issn
0367-8377
pubmed:author
pubmed:issnType
Print
pubmed:volume
31
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
335-8
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed:year
1988
pubmed:articleTitle
N-terminal sequences of gamma-crystallins from the amphibian lens and their homology with gamma-crystallins of other major classes of vertebrates.
pubmed:affiliation
Institute of Biochemical Sciences, National Taiwan University, Taipei, R.O.C.
pubmed:publicationType
Journal Article, Comparative Study, Research Support, Non-U.S. Gov't