Linked Life Data

7346378

Source:http://linkedlifedata.com/resource/pubmed/id/7346378

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
8
pubmed:dateCreated
1982-10-21
pubmed:abstractText
The alpha- and beta-chains of the main component of hemoglobin of the greylag goose (Anser anser) were isolated. For determination of the primary structure of hemoglobin, the chains were cleaved and the cleavage products isolated. The chains and peptides were degraded automatically in the sequenator: the complete primary structure of the alpha-and beta-chains was obtained and compared with the human adult hemoglobin. Comparison with human sequences show 1 substitutions in the alpha-chain and 44 in beta-chain. The mutations are discussed. The alpha-chains contain no tryptophan, only one methionine and two cysteines. Seven alpha 1 beta 1-contacts and one alpha 1 beta 2-oxy- and deoxy-contact are altered. In the beta-chains two acidic amino acids are eliminated. This is probably the reason for the more basic character of the greylag goose hemoglobin. The contact points of the allosteric effector (inositol pentaphosphate in case of birds, 2,3-diphosphoglycerate in case of mamals) with the beta-chains are identical in chicken and greylag goose, two more than in the human beta-chains. Six alpha 1 beta 1-contacts and one hem-contact are changed. This work forms a basis to allow comparison of the functions of several bird hemoglobins and for further studies of bird hemoglobins and for further studies of evolution and systematics of birds.
pubmed:language
ger
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Aug
pubmed:issn
0018-4888
pubmed:author
pubmed:issnType
Print
pubmed:volume
362
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
1101-12
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed:year
1981
pubmed:articleTitle
[Hemoglobins, XLII: Studies on the hemoglobin of the greylag goose (Anser anser). The primary structures of the alpha- and beta-chains of the main component (author's transl)].
pubmed:publicationType
Journal Article, English Abstract