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|Type:||Artigo de periódico|
|Title:||cDNA-derived amino-acid sequence of a land turtle (Geochelone carbonaria) beta-chain hemoglobin.|
|Abstract:||The cDNA sequence encoding the turtle Geochelone carbonaria beta-chain was determinated. The isolation of hemoglobin mRNA was based on degenerate primers' PCR in combination with 5'- and 3'-RACE protocol. The full length cDNA is 615 bp with the ATG start codon at position 53 and TGA stop codon at position 495; The AATAAA polyadenylation signal is found at position 599. The deduced polypeptyde contains 146 amino-acid residues. The predicted amino acid sequence shares 83% identity with the beta-globin of a related specie, the aquatic turtle C. p. belli. Otherwise, identity is higher when compared with chicken beta-Hb (80%) than with other reptilian orders (Squamata, 69%, and Crocodilia, 61%). Compared with human HbA, there is 67% identity, and at least three amino acid substitutions could be of some functional significance (Glu43 beta-->Ser, His 116 beta--> Thr and His143 beta-->Leu). To our knowledge this represents the first cDNA sequence of a reptile globin gene described.|
|Editor:||Academic Press Aust|
|Citation:||Biochemistry And Molecular Biology International. Academic Press Aust, v. 42, n. 2, n. 255, n. 260, 1997.|
|Appears in Collections:||Unicamp - Artigos e Outros Documentos|
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