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Characterization of hemoglobin from the lizard Uromastix hardwickii
Author(s) -
Naqvi Sabira,
Zaidi Zafar H.,
von Bahr-Lindström Hedvig,
Carlquist Mats,
Jörnvall Hans
Publication year - 1983
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(83)80774-1
Subject(s) - globin , hemoglobin , trypsin , chemistry , homology (biology) , peptide sequence , lizard , chromatography , biochemistry , amino acid , biology , enzyme , zoology , gene
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.