Characterization and function of isolated hemoglobins from the tuatara, Sphenodon Punctatus (Reptilia: O. Rhynchocephalia)

• Published in: Comparative biochemistry and physiology. B, Comparative biochemistry Vol. 79; no. 1; pp. 119 - 123
• Main Authors: Tetens, V., Brittain, T., Christie, D.L., Robb, J., Wells, R.M.G.
• Format: Journal Article
• Language: English
• Published: New York, NY Elsevier Inc 1984; Elsevier Science
• Subjects: Analytical, structural and metabolic biochemistry; Biological and medical sciences; erythrocytes; Fundamental and applied biological sciences. Psychology; hemoglobin; Hemoproteins; isoelectric focusing; Metalloproteins; Proteins; Sphenodon punctatus; Vertebrata; Hemoprotein; Oxygen; Structure activity relation; Bohr effect; Gel electrophoresis; Hemoglobin; Dissociation constant; Reptilia
• ISSN: 0305-0491
• DOI: 10.1016/0305-0491(84)90086-5

1. 1. Three hemoglobin (Hb) components were identified from the red blood cells of Sphenodon using polyacrylamide gel electrophoresis and isoelectric focusing. 2. 2. Five globin chain types were identified by both isoelectric focusing following PCMB treatment and by HPLC separation. Two of the Hbs appeared to share a common chain and the structures are envisaged as Hb I (a 2b 2), Hb II (c 2d 2) and Hb III (c 2e 2). 3. 3. O 2 equilibria of Hb fractions isolated by preparative isoelectric focusing showed low cooperativity (n ⋍ 1.2) and small Bohr constants ( Φ = Δlog P 50/ ΔpH) of −0.02 to −0.14. 4. 4. Stopped-flow oxygen-dissociation kinetics indicated kinetic equivalence of the α and β-type subunits.