Linked Life Data

8262931

Source:http://linkedlifedata.com/resource/pubmed/id/8262931

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
36
pubmed:dateCreated
1994-1-27
pubmed:databankReference
pubmed:abstractText
The adult bullfrog (Rana catesbeiana) has two major tetrameric hemoglobins, B and C, which share a common beta chain but have different alpha chains. Components B and C associate upon deoxygenation to form a complex of the form BC2, a trimer of tetramers that depends on contacts between the alpha B and alpha C chains. Nucleotide sequences of cDNA transcripts for these chains have been determined. Transcripts were identified by analysis of the amino acid compositions of the tryptic peptides of the components and by partial amino acid sequencing. These results, together with the amino acid sequence of the beta chain (Tam, L.-T., Gray, G. P., and Riggs, A. F. (1986) J. Biol. Chem. 261, 8290-8294), permit an analysis of the structures of the alpha 2 beta 2 tetramers of hemoglobins B and C. Molecular modeling suggests possible residues at the alpha B-alpha C interfaces in the BC2 trimer and additional alpha C-alpha C contacts that would form a closed ring of six alpha chain subunits that would further stabilize the BC2 trimer. Phylogenetic analysis of the alpha B sequence suggests that it may be a "tadpole" chain, the temporal expression of which has shifted from larva to adult.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Dec
pubmed:issn
0021-9258
pubmed:author
pubmed:issnType
Print
pubmed:day
25
pubmed:volume
268
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
26961-71
pubmed:dateRevised
2007-11-14
pubmed:meshHeading
pubmed:year
1993
pubmed:articleTitle
The hemoglobins of the bullfrog, Rana catesbeiana. The cDNA-derived amino acid sequences of the alpha chains of adult hemoglobins B and C: their roles in deoxygenation-induced aggregation.
pubmed:affiliation
Department of Biochemistry and Molecular Biology, University of Oklahoma Health Sciences Center, Oklahoma City 73190.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S., Research Support, U.S. Gov't, Non-P.H.S., Research Support, Non-U.S. Gov't