Hämoglobine, XXXVII. Die Primärstruktur eines monomeren Insektenhämoglobins (Erythrocruorin), Komponente CTT IIIa vonChironomus thummi thummi.Ein ungewöhnlicher Hämkomplex: E7 Gln, E11 Ile.

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Abstract
The primary structure of the monomeric HB CTT IIIa of the midge larva of C. t. thummi is presented. Cyanogenbromide peptides and tryptic peptides were used for sequence analysis. The primary structure was established with a small number of large peptides. The complete sequencing of the cyanogen bromide peptides was enabled by the C-terminal fixation of arginine. The primary structure of CTT IIIa is compared to the .beta.-chains of human and to the monomeric component CTT III: CTT IIIa possesses a tail of 9 amino acids on the N-terminus, and shows only a small number of identical residues compared to the number that other CTT hemoglobins share with each other. Also the heme complex is unusual: E7 glycine and E11 isoleucine.

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