Characterization of hemoglobin from the lizard Uromastix hardwickii

• Published in: FEBS letters Vol. 162; no. 2; pp. 290 - 295
• Main Authors: Naqvi, Sabira, Zaidi, Zafar H., von Bahr-Lindström, Hedvig, Carlquist, Mats, Jörnvall, Hans
• Format: Journal Article
• Language: English
• Published: Amsterdam Elsevier B.V 17.10.1983; Elsevier
• Subjects: Amino Acid Sequence; Amino acid sequence analysis; Analytical, structural and metabolic biochemistry; Animals; Biological and medical sciences; Chemical Phenomena; Chemistry; Fundamental and applied biological sciences. Psychology; hemoglobin; Hemoglobin heterogeneity; Hemoglobins - isolation & purification; Hemoproteins; Homology; Lizards - blood; Metalloproteins; Peptide Fragments; Proteins; Uromastix hardwickii; Amino acid sequence analysis; Homology; Hemoglobin heterogeneity; Vertebrata; Sauria; Biological evolution; Beta-Peptide chain; Hemoglobin; Alpha-Peptide chain; Reptilia; Peptide chain; Ophidia
• ISSN: 0014-5793; 1873-3468
• DOI: 10.1016/0014-5793(83)80774-1

Hemoglobin from the tropic lizard Uromastix hardwickii was isolated. Chain separations were studied, and the whole carboxymethylated globin was cleaved with trypsin. Peptides were pre-fractionated by exclusion chromatography and finally purified by reversed phase high-performance liquid chromatography. Amino acid sequence analysis permitted ordering of peptides in α- and β-chains by homology with known structures in other hemoglobins. Results show large structural variations (about 50% homology between Uromastix and viper α-chains) and suggest chain heterogeneity with the presence of at least two types of both the α- and β-chains in the preparations.