Biomaterial Database

[Hemoglobins, XXV. Hemoglobin (erythrocruorin) CTT III from Chironomus thummi thummi (Diptera). Primary structure and relationship to other heme proteins (author's transl)]. 1979

G Buse, and G J Steffens, and G Braunitzer, and W Steer

The amino acid sequence analysis of hemoglobin (erythrocruorin) CTT III from Chironomus thummi th. (Diptera) has been checked with automatic methods and completed. The protein chain consists of 136 amino acids and contains a neutral exchange isoleucine/threonine in position 57. The molecular weight of the heme protein (Thr) is 15400. The primary structure gives the chemical basis for the refinement of the X-ray structure and the understanding of the mechanism of the Bohr effect in this monomeric hemoglobin. A homologous alignment to vertebrate globins is reported. The resulting data for the phylogeny of proto-and deuterostomian animals and the function of this hemoglobin are discussed.

UI	MeSH Term	Description	Entries
D008970	Molecular Weight	The sum of the weight of all the atoms in a molecule.	Molecular Weights,Weight, Molecular,Weights, Molecular
D004175	Diptera	An order of the class Insecta. Wings, when present, number two and distinguish Diptera from other so-called flies, while the halteres, or reduced hindwings, separate Diptera from other insects with one pair of wings. The order includes the families Calliphoridae, Oestridae, Phoridae, SARCOPHAGIDAE, Scatophagidae, Sciaridae, SIMULIIDAE, Tabanidae, Therevidae, Trypetidae, CERATOPOGONIDAE; CHIRONOMIDAE; CULICIDAE; DROSOPHILIDAE; GLOSSINIDAE; MUSCIDAE; TEPHRITIDAE; and PSYCHODIDAE. The larval form of Diptera species are called maggots (see LARVA).	Flies, True,Flies,Dipteras,Fly,Fly, True,True Flies,True Fly
D004902	Erythrocruorins	High molecular weight (1,500,000 to 3,000,000) hemoglobins found in the plasma of many polychete and oligochete annelid worms, crustaceans, insects, and mollusks. They bind one mole of oxygen per heme and function as oxygen carriers.
D006420	Hemeproteins	Proteins that contain an iron-porphyrin, or heme, prosthetic group resembling that of hemoglobin. (From Lehninger, Principles of Biochemistry, 1982, p480)	Hemeprotein,Heme Protein,Heme Proteins,Protein, Heme,Proteins, Heme
D006454	Hemoglobins	The oxygen-carrying proteins of ERYTHROCYTES. They are found in all vertebrates and some invertebrates. The number of globin subunits in the hemoglobin quaternary structure differs between species. Structures range from monomeric to a variety of multimeric arrangements.	Eryhem,Ferrous Hemoglobin,Hemoglobin,Hemoglobin, Ferrous
D006801	Humans	Members of the species Homo sapiens.	Homo sapiens,Man (Taxonomy),Human,Man, Modern,Modern Man
D000595	Amino Acid Sequence	The order of amino acids as they occur in a polypeptide chain. This is referred to as the primary structure of proteins. It is of fundamental importance in determining PROTEIN CONFORMATION.	Protein Structure, Primary,Amino Acid Sequences,Sequence, Amino Acid,Sequences, Amino Acid,Primary Protein Structure,Primary Protein Structures,Protein Structures, Primary,Structure, Primary Protein,Structures, Primary Protein
D000818	Animals	Unicellular or multicellular, heterotrophic organisms, that have sensation and the power of voluntary movement. Under the older five kingdom paradigm, Animalia was one of the kingdoms. Under the modern three domain model, Animalia represents one of the many groups in the domain EUKARYOTA.	Animal,Metazoa,Animalia
D013045	Species Specificity	The restriction of a characteristic behavior, anatomical structure or physical system, such as immune response; metabolic response, or gene or gene variant to the members of one species. It refers to that property which differentiates one species from another but it is also used for phylogenetic levels higher or lower than the species.	Species Specificities,Specificities, Species,Specificity, Species