Hämoglobine,XXXl. Analyse der Primärstruktur des monomeren Insektenhämoglobins CTT I. (Erythrocruorin) ausChironomus thummi thummi, Diptera

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Abstract
The sequence analysis of the monomeric hemoglobin CTT I (erythrocruorin) of C. t. thummi is given. The tryptic peptides were separated and sequenced by automatic Edman degradation. Alignment was established with the help of some peptic peptides. In CTT I two polypeptide chains are present. They differ in position 98, where alanine and threonine occurred 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, because CTT I seems to have an enlarged heme pocket like them. The amino acid residues involved in the heme contacts are compared. The lack of a Bohr effect is discussed.

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