THE PRIMARY STRUCTURE OF THE HEMOGLOBIN FROM THE LOBE-LIPPED BAT (CHALINOLOBOS-MORIO, MICROCHIROPTERA)

The hemoglobin of the lobe-lipped bat (Chalinolobus morio, Vespertilio nidae) is composed of 45% HbI and 55% HbII. Both components show ident ical alpha-chains but differ at the following three positions of their beta-chains: beta I/beta II 21: Glu/Asp, 70: Ser/Ala, and 135: Gin/Le u. High performance liquid chromatography revealed pure alpha-chains a nd a mixture of only partly separated beta-chains. Based on this mater ial, the primary structures of all three globin chains could be achiev ed by automatic Edman degradation of the whole chains and peptides obt ained by trypsin hydrolysis. Compared to human hemoglobin, Chalinolobu s shows 17 replacements in the alpha-chains and 24/22 in the beta-chai ns. A sequence comparison of the globin chains from the three vesperti lionid bats Chalinolobus morio and Myotis velifer (Vespertilioninae) a s well as Antrozous pallidus (Nyctophilinae) supports a close relation ship of the former only for the beta-chains. Molecular modeling showed that the replacements involved in three alpha 1/beta 1 and one alpha 1/beta 2 subunit interface contacts do not cause any interruption. All phosphate binding sites and amino acid residues responsible for the B ohr effect are unchanged. Thus normal physiological properties should be expected for Chalinolobus morio hemoglobin.