title: Characterization of hemoglobin from the lizard Uromastix hardwickii.
abstract: 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 alpha- and beta-chains by homology with known structures in other hemoglobins. Results show large structural variations (about 50% homology between Uromastix and viper alpha-chains) and suggest chain heterogeneity with the presence of at least two types of both the alpha- and beta-chains in the preparations.
mesh_terms: D000595:Amino Acid Sequence; D000818:Animals; D055598:Chemical Phenomena; D002621:Chemistry; D006454:Hemoglobins / Q000302:isolation & purification*; D008116:Lizards / Q000097:blood*; D010446:Peptide Fragments
chemical_list: D006454:Hemoglobins; D010446:Peptide Fragments