A: The Rimary Structure of Hemoglobins From Two Carnivora:1 Lion (Panthera Leo), 2 Tiger (Panthera Tigris)B: Classical Synthesis of Thymosin β9 (1-4,22-24, 33-41)

Abstract

The complete primary structure of hemoglobin from lion (Panthera leo) and tiger (Panthera tigris) has been determined. Globin of both animals contain two components identified to be HbI and HbII. The 8 chains of the two animals are identical while they differ in their chains. Native globin chains Were separated on ion-exchange and RP-HPLC column. The sequence of the globin chains as well as tryptic -peptides was studied by automatic Edman degradation methods using liquid-phase sequencer and gas-phase sequencer. The intact subunits Were digested by enzymatic cleavage into tryptic peptides. The sequences Were compared for homology with human hemoglobin. The β-chain of the major components (βI) has a blocked N-terminal residue, identified as acetylated serine, whereas that of the minor component (β II) is free glycine. The two hemoglobin components of lion as well as tiger have identical צ chains and differ with respect to their β-chains at the following positions (βI/βII/): ,NA1 Ac-Ser/Gly, 8A1 Ser/Thr, β H17 Ser/ Asn and 8HC1 Arg/Lys. The structural and functional aspects of these exchanges are discussed. Homologous alignment of the structure with 14 other animals belonging to different families of order carnivora discloses many interesting points.