Linked Life Data

3228493

Source:http://linkedlifedata.com/resource/pubmed/id/3228493

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
9
pubmed:dateCreated
1989-4-14
pubmed:abstractText
The primary structures of the hemoglobins of two Flying Foxes of the genus Pteropus are presented. Both comprise two components: in P. alecto hemoglobin two alpha-chains at a ratio of 1:1 and two beta-chains at a ratio of 4:1 were detected. The hemoglobin of P. poliocephalus comprises one alpha-chain and two beta-chains, the latter at a ratio of 1:1. The globin chains were separated by high-performance liquid chromatography and the sequences determined by automatic liquid and gas phase Edman degradation of the chains and their tryptic peptides. Compared with human hemoglobin, the alpha-chains of P. alecto and P. poliocephalus show 18 and 19 exchanges, respectively, whereas in the beta-chains 16/17 substitutions are found in both cases. In the alpha-chains of P. alecto, one exchange involves an alpha 1/beta 1-contact. In the beta-chains of both species one heme-, one alpha 1/beta 2- and two alpha 1/beta 1-contacts are exchanged. The relevant side chains are the same in both species. The functional and systematic aspects of these findings are discussed.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Sep
pubmed:issn
0177-3593
pubmed:author
pubmed:issnType
Print
pubmed:volume
369
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
975-84
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed:year
1988
pubmed:articleTitle
The primary structure of the hemoglobin from the grey-headed flying fox (Pteropus poliocephalus) and the black flying fox (P. alecto, Megachiroptera).
pubmed:affiliation
Max-Planck-Institut für Biochemie, Abteilung Proteinchemie, Martinsried bei München.
pubmed:publicationType
Journal Article, Comparative Study, Research Support, Non-U.S. Gov't