[Hemoglobin, XXXI. Analysis or the primary structure of the monomeric hemoglobin CTT I (erythrocruorin) of Chironomus thummi thummi, Diptera].

The sequence analysis of the monomeric hemoglobin CTT I (erythrocruorin) of Chironomus thummi thummi is given. The tryptic peptides were separated and sequenced by automatic Edman degradation. The alignment was established with help of some peptic peptides. In CTT I two polypeptide chains are present. They differ in position 98, where we found alanine and threonine in the ratio 1:1. CTT I is compared with human myoglobin and the monomeric component CTT III. The dimeric components of CTT are also included into the discussion, because CTT I seems to have an enlarged heme pocket like them. We particularly compare the amino acid residues involved in the heme contacts. The lack of a Bohr effect is discussed.