Abstract
The complete primary structure of the major hemoglobin component from the adult European lynx (Lynx lynx) is presented. Presence of two hemoglobin components and three chains, βA, βB, and α, identified by gel electrophoresis. The purification of the globin chains achieved by ion-exchange chromatography. The globin chains were digested with trypsin. The peptide generated were purified by reversed-phase HPLC. Sequencing of the native chains up to 42 cycles and of the tryptic peptides were deduced by Edman degradation in liquid- and gasphase sequencer. The primary structure established aligned with those of human Hb-A. The comparison of lynx globin chains with other representatives of the Felidae, lion, tiger, jaguar, leopard, and cat revealed high homology.
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Ahmed, A., Jahan, M. & Braunitzer, G. Carnivora: The primary structure of the major hemoglobin component from adult European lynx (Lynx lynx, Felidae). J Protein Chem 11, 39–43 (1992). https://doi.org/10.1007/BF01025090
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DOI: https://doi.org/10.1007/BF01025090