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Hemo globins part 25 hemo globin erythrocruorin ctt iii chironomus thummi thummi diptera primary structure and relationship to other heme proteins



Hemo globins part 25 hemo globin erythrocruorin ctt iii chironomus thummi thummi diptera primary structure and relationship to other heme proteins



Hoppe-Seyler's Zeitschrift fuer Physiologische Chemie 360(1): 89-98



The amino acid sequence analysis of Hb (erythrocruorin) CTT III from C. thummi thummi (Diptera) was 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 MW of the heme protein (Thr) is 15,400. 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 Hb. A homologous alignment to vertebrate globins is reported. The resulting data for the phylogeny of proto and deuterostomian animals and the function of this Hb are discussed.

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Accession: 005556087

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