[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.
D000595:Amino Acid Sequence; D000818:Animals; D004175:Diptera / Q000032:analysis*; D004902:Erythrocruorins; D006454:Hemoglobins; D010446:Peptide Fragments / Q000032:analysis; D014357:Trypsin
D004902:Erythrocruorins; D006454:Hemoglobins; D010446:Peptide Fragments; D014357:Trypsin
Hämoglobine, XXXI. Analyse der Primärstruktur des monomeren Insektenhämoglobins CTT I (Erythrocruorin) aus Chironomus thummi thummi, Dipera.