[Hemoglobins XL: Sequence analysis of the monomeric hemoglobin CTT IV (erythrocruorin) of Chironomus thummi thummi, Diptera (author's transl)].
The sequence analysis of the monomeric hemoglobin CTT IV is given. The primary structure was determined by automatic Edman degradation of the protein and of peptides obtained by enzymatical or by chemical cleavages. The protein chain consists of 136 amino acids. The primary structure is compared with the primary structure of the human beta-chains and of the monomeric hemoglobin CTT III.
D000595:Amino Acid Sequence; D002683:Chironomidae / Q000032:analysis*; D003488:Cyanogen Bromide; D004175:Diptera / Q000032:analysis*; D004902:Erythrocruorins; D006454:Hemoglobins; D006801:Humans; D010446:Peptide Fragments / Q000032:analysis; D013045:Species Specificity; D014357:Trypsin
D004902:Erythrocruorins; D006454:Hemoglobins; D010446:Peptide Fragments; D014357:Trypsin; D003488:Cyanogen Bromide
Hämoglobine, XL. Sequenzanalyse des monomeren Insektenhämoglobins CTT IV (Erythrocruorin) aus Chironomus thummi thummi (Diptera).