The primary structure of the hemoglobin from the bat Macrotus californicus (Chiroptera)

The complete primary structure of the hemoglobin from the bat Macrotus californicus (Chiroptera) is presented. This hemoglobin consists of only one component. The alpha- and beta-chains were separated by reverse phase high performance liquid chromatography. The sequences of both chains were established by automatic Edman degradation of the chains and the tryptic peptides, as well as of the C-terminal peptide obtained by acidic hydrolysis of the Asp-Pro bond in the beta-chains using the film- and gas-phase method. The sequences are compared with human hemoglobin: 15 amino-acid substitutions are found in the alpha- and 22 in the beta-chains. A comparison with the hemoglobin of Rousettus aegyptiacus and Myotis velifer shows a closer relation to the Mega- than to the Microchiroptera.