Abstract

The complete primary structure of the two hemoglobin components of the adult North Persian Leopard are presented. The major component Hb-I accounts for 80-90% and the minor component Hb-II accounts for 20-10% of the total hemoglobin. Reversed phase HPLC was used for the separation of the polypeptide chains. The amino acid sequences were established by automated Edman degradation of the globin chains and of the tryptic peptides in liquid-and gas-phase sequenators. The sequences are aligned with those of human Hb-A. Our result shows that the hemoglobins of North Persian Leopard and Jaguar are identical in amino acid sequence.

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