Characterization of hemoglobin from the lizard Uromastix hardwickii

FEBS Letters

von Bahr-Lindström, Hedvig¹  Naqvi, Sabira¹  Zaidi, Zafar H.¹  Carlquist, Mats¹  Jörnvall, Hans¹ 

[1] Departments of Chemistry I and Biochemistry II, Karolinska Institutet, S-104 01 Stockholm, Sweden

关键词: Hemoglobin heterogeneity;    Amino acid sequence analysis;    Homology;   

DOI  :  10.1016/0014-5793(83)80774-1

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

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.

【 授权许可】

Unknown