Biomaterial Database

[Hemoglobin, XXXI. Analysis or the primary structure of the monomeric hemoglobin CTT I (erythrocruorin) of Chironomus thummi thummi, Diptera]. 1980

T Kleinschmidt, and H von der Mark-Neuwirth, and G Braunitzer

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.

UI	MeSH Term	Description	Entries
D010446	Peptide Fragments	Partial proteins formed by partial hydrolysis of complete proteins or generated through PROTEIN ENGINEERING techniques.	Peptide Fragment,Fragment, Peptide,Fragments, Peptide
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.
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
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
D014357	Trypsin	A serine endopeptidase that is formed from TRYPSINOGEN in the pancreas. It is converted into its active form by ENTEROPEPTIDASE in the small intestine. It catalyzes hydrolysis of the carboxyl group of either arginine or lysine. EC 3.4.21.4.	Tripcellim,Trypure,beta-Trypsin,beta Trypsin