Switch to
Predicate | Object |
---|---|
rdf:type | |
lifeskim:mentions | |
pubmed:issue |
1-2
|
pubmed:dateCreated |
1991-5-8
|
pubmed:abstractText |
The complete amino acid sequences of chicken and turkey beta 2-microglobulins have been determined by analyses of tryptic, V8-proteolytic and cyanogen bromide fragments, and by N-terminal sequencing. Mass spectrometric analysis of chicken beta 2-microglobulin supports the sequence-derived Mr of 11,048. The higher apparent Mr obtained for the avian beta 2-microglobulins as compared to human beta 2-microglobulin by SDS-PAGE is not understood. Chicken and turkey beta 2-microglobulin consist of 98 residues and deviate at seven positions: 60, 66, 74-76, 78 and 82. The chicken and turkey sequences are identical to human beta 2-microglobulin at 46 and 47 positions, respectively, and to bovine beta 2-microglobulin at 47 positions, i.e. there is about 47% identity between avian and mammalian beta 2-microglobulins. The known X-ray crystallographic structures of bovine beta 2-microglobulin and human HLA-A2 complex suggest that the seven chicken to turkey differences are exposed to solvent in the avian MHC class I complex. The key residues of beta 2-microglobulin involved in alpha chain contacts within the MHC class I molecule are highly conserved between chicken and man. This explains that heterologous human beta 2-microglobulin can substitute the chicken beta 2-microglobulin in exchange studies with B-F (chicken MHC class I molecule), and suggests that the MHC class I structure is conserved over long evolutionary distances.
|
pubmed:language |
eng
|
pubmed:journal | |
pubmed:citationSubset |
IM
|
pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Peptide Fragments,
http://linkedlifedata.com/resource/pubmed/chemical/Serine Endopeptidases,
http://linkedlifedata.com/resource/pubmed/chemical/Trypsin,
http://linkedlifedata.com/resource/pubmed/chemical/beta 2-Microglobulin,
http://linkedlifedata.com/resource/pubmed/chemical/glutamyl endopeptidase
|
pubmed:status |
MEDLINE
|
pubmed:issn |
0161-5890
|
pubmed:author | |
pubmed:issnType |
Print
|
pubmed:volume |
28
|
pubmed:owner |
NLM
|
pubmed:authorsComplete |
Y
|
pubmed:pagination |
177-82
|
pubmed:dateRevised |
2006-11-15
|
pubmed:meshHeading |
pubmed-meshheading:2011126-Amino Acid Sequence,
pubmed-meshheading:2011126-Animals,
pubmed-meshheading:2011126-Chickens,
pubmed-meshheading:2011126-Chromatography, High Pressure Liquid,
pubmed-meshheading:2011126-Isoelectric Point,
pubmed-meshheading:2011126-Mass Spectrometry,
pubmed-meshheading:2011126-Molecular Sequence Data,
pubmed-meshheading:2011126-Molecular Weight,
pubmed-meshheading:2011126-Oxidation-Reduction,
pubmed-meshheading:2011126-Peptide Fragments,
pubmed-meshheading:2011126-Serine Endopeptidases,
pubmed-meshheading:2011126-Trypsin,
pubmed-meshheading:2011126-Turkeys,
pubmed-meshheading:2011126-beta 2-Microglobulin
|
pubmed:articleTitle |
Amino acid sequences and structures of chicken and turkey beta 2-microglobulin.
|
pubmed:affiliation |
Institute of Biochemical Genetics, University of Copenhagen, Denmark.
|
pubmed:publicationType |
Journal Article,
Comparative Study,
Research Support, Non-U.S. Gov't
|