Characterization of hemoglobin from the lizard Uromastix hardwickii |
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Authors: | Sabira Naqvi Zafar H Zaidi Hedvig von Bahr-Lindström Mats Carlquist Hans Jörnvall |
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Institution: | Departments of Chemistry I and Biochemistry II, Karolinska Institutet, S-104 01 Stockholm, Sweden;HEJ Research Institute of Chemistry, University of Karachi, Karachi, Pakistan |
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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. |
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Keywords: | Hemoglobin heterogeneity Amino acid sequence analysis Homology |
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