AMINO ACID SEQUENCE OF HEMOGLOBIN COMPONENT FROM COLUMBA LIVIA (GERY PIGEON)

Abstract

The primary structure of hemoglobin from Grey Wild Pigeon (Columba livia) has been investigated. This is the first sequence determination study of the order Columbiformes. Native globin was separated on ion exchanger and reversed phase high performance liquid chromatography. The intact subunits were further degraded by enzymatic and chemical cleavage into peptides. The structure of hemoglobin was established by sequence determination of tryptic peptides manually as well as automatically on Gas-phase sequencer. Homologous alignment of the structure with twenty other bird species belonging to different order indicate many interesting points. Among the different exchanges, positions α24 Leu, α26 Gly , α32 Leu, α64 Glu , α111 Ala, α113 Phe and α129 Val, β14, Ile, β55 ser, β59Asn, β61 Lys and β83 Gly are unique to pigeon hemoglobin. The various exchanges are discussed with reference to physiology closer to the order Anseriformes. On the basis of sequence data the phylogenic placement of Columba livia could be established among the birds having single hemoglobin component. The evolutionary relationship between mammals, birds and reptiles (Crocodiles) is discussed.