The hemoglobins of the bullfrog, Rana catesbeiana - The cDNA-derived amino acid sequences of the α chains of adult hemoglobins B and C

Their roles in deoxygenation-induced aggregation

David J. Smith, Hao Zhu, Prasanna Kolatkar, Lei Ting Tam, Thomas O. Baldwin, Bruce A. Roe, Robert H. Broyles, Austen F. Riggs

Research output: Contribution to journalArticle

11 Citations (Scopus)

Abstract

The adult bullfrog (Rana catesbeiana) has two major tetrameric hemoglobins, B and C, which share a common β chain but have different α 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 αB and αC 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 β 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 α2β2 tetramers of hemoglobins B and C. Molecular modeling suggests possible residues at the αBC interfaces in the BC2 trimer and additional αCC contacts that would form a closed ring of six α chain subunits that would further stabilize the BC2 trimer. Phylogenetic analysis of the αB sequence suggests that it may be a "tadpole" chain, the temporal expression of which has shifted from larva to adult.

Original languageEnglish
Pages (from-to)26961-26971
Number of pages11
JournalJournal of Biological Chemistry
Volume268
Issue number36
Publication statusPublished - 25 Dec 1993
Externally publishedYes

Fingerprint

Hemoglobin C
Rana catesbeiana
Larva
Amino Acid Sequence
Hemoglobins
Agglomeration
Complementary DNA
Amino Acids
Protein Sequence Analysis
Sequence Analysis
Molecular modeling
Peptides
Nucleotides
Chemical analysis
hemoglobin B

ASJC Scopus subject areas

  • Biochemistry

Cite this

The hemoglobins of the bullfrog, Rana catesbeiana - The cDNA-derived amino acid sequences of the α chains of adult hemoglobins B and C : Their roles in deoxygenation-induced aggregation. / Smith, David J.; Zhu, Hao; Kolatkar, Prasanna; Tam, Lei Ting; Baldwin, Thomas O.; Roe, Bruce A.; Broyles, Robert H.; Riggs, Austen F.

In: Journal of Biological Chemistry, Vol. 268, No. 36, 25.12.1993, p. 26961-26971.

Research output: Contribution to journalArticle

Smith, David J. ; Zhu, Hao ; Kolatkar, Prasanna ; Tam, Lei Ting ; Baldwin, Thomas O. ; Roe, Bruce A. ; Broyles, Robert H. ; Riggs, Austen F. / The hemoglobins of the bullfrog, Rana catesbeiana - The cDNA-derived amino acid sequences of the α chains of adult hemoglobins B and C : Their roles in deoxygenation-induced aggregation. In: Journal of Biological Chemistry. 1993 ; Vol. 268, No. 36. pp. 26961-26971.
@article{709cd4856f7b49889706a0fa7f80f982,
title = "The hemoglobins of the bullfrog, Rana catesbeiana - The cDNA-derived amino acid sequences of the α chains of adult hemoglobins B and C: Their roles in deoxygenation-induced aggregation",
abstract = "The adult bullfrog (Rana catesbeiana) has two major tetrameric hemoglobins, B and C, which share a common β chain but have different α 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 αB and αC 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 β 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 α2β2 tetramers of hemoglobins B and C. Molecular modeling suggests possible residues at the αB-αC interfaces in the BC2 trimer and additional αC-αC contacts that would form a closed ring of six α chain subunits that would further stabilize the BC2 trimer. Phylogenetic analysis of the αB sequence suggests that it may be a {"}tadpole{"} chain, the temporal expression of which has shifted from larva to adult.",
author = "Smith, {David J.} and Hao Zhu and Prasanna Kolatkar and Tam, {Lei Ting} and Baldwin, {Thomas O.} and Roe, {Bruce A.} and Broyles, {Robert H.} and Riggs, {Austen F.}",
year = "1993",
month = "12",
day = "25",
language = "English",
volume = "268",
pages = "26961--26971",
journal = "Journal of Biological Chemistry",
issn = "0021-9258",
publisher = "American Society for Biochemistry and Molecular Biology Inc.",
number = "36",

}

TY - JOUR

T1 - The hemoglobins of the bullfrog, Rana catesbeiana - The cDNA-derived amino acid sequences of the α chains of adult hemoglobins B and C

T2 - Their roles in deoxygenation-induced aggregation

AU - Smith, David J.

AU - Zhu, Hao

AU - Kolatkar, Prasanna

AU - Tam, Lei Ting

AU - Baldwin, Thomas O.

AU - Roe, Bruce A.

AU - Broyles, Robert H.

AU - Riggs, Austen F.

PY - 1993/12/25

Y1 - 1993/12/25

N2 - The adult bullfrog (Rana catesbeiana) has two major tetrameric hemoglobins, B and C, which share a common β chain but have different α 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 αB and αC 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 β 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 α2β2 tetramers of hemoglobins B and C. Molecular modeling suggests possible residues at the αB-αC interfaces in the BC2 trimer and additional αC-αC contacts that would form a closed ring of six α chain subunits that would further stabilize the BC2 trimer. Phylogenetic analysis of the αB sequence suggests that it may be a "tadpole" chain, the temporal expression of which has shifted from larva to adult.

AB - The adult bullfrog (Rana catesbeiana) has two major tetrameric hemoglobins, B and C, which share a common β chain but have different α 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 αB and αC 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 β 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 α2β2 tetramers of hemoglobins B and C. Molecular modeling suggests possible residues at the αB-αC interfaces in the BC2 trimer and additional αC-αC contacts that would form a closed ring of six α chain subunits that would further stabilize the BC2 trimer. Phylogenetic analysis of the αB sequence suggests that it may be a "tadpole" chain, the temporal expression of which has shifted from larva to adult.

UR - http://www.scopus.com/inward/record.url?scp=0027724107&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=0027724107&partnerID=8YFLogxK

M3 - Article

VL - 268

SP - 26961

EP - 26971

JO - Journal of Biological Chemistry

JF - Journal of Biological Chemistry

SN - 0021-9258

IS - 36

ER -