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J Protein Chem. 1992 Feb;11(1):39-43.

Carnivora: the primary structure of the major hemoglobin component from adult European lynx (Lynx lynx, Felidae).

Author information

1
Max-Planck Institut für Biochemie, Abt. Proteinchemie, Martinsried, bei München, Germany.

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, beta A, beta B, and alpha, 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 gas-phase 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.

PMID:
1515033
DOI:
10.1007/bf01025090
[Indexed for MEDLINE]

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