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

• Published in: The Journal of biological chemistry Vol. 268; no. 36; pp. 26961 - 26971
• Main Authors: Smith, D J, Zhu, H, Kolatkar, P R, Tam, L T, Baldwin, T O, Roe, B A, Broyles, R H, Riggs, A F
• Format: Journal Article
• Language: English
• Published: Bethesda, MD Elsevier Inc 25.12.1993; American Society for Biochemistry and Molecular Biology
• Subjects: Amino Acid Sequence; Analytical, structural and metabolic biochemistry; Animals; Base Sequence; Biological and medical sciences; Cloning, Molecular; DNA, Complementary; Freshwater; Fundamental and applied biological sciences. Psychology; Hemoglobins - genetics; Hemoglobins - metabolism; Hemoproteins; Metalloproteins; Molecular Sequence Data; Oxygen - metabolism; Phylogeny; Protein Conformation; Proteins; Rana catesbeiana; Sequence Homology, Amino Acid; Aggregation; Hemoprotein; Vertebrata; Amphibia; Hemoglobin; Molecular interaction; Primary structure; Salientia; Peptide chain; Molecular cloning; Rana catesbeiana

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...