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Type: Artigo de periódico
Title: cDNA-derived amino-acid sequence of a land turtle (Geochelone carbonaria) beta-chain hemoglobin.
Author: Bordin, S
Meza, AN
Saad, STO
Ogo, SH
Costa, FF
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.
Subject: hemoglobins
cDNA cloning
Country: Australia
Editor: Academic Press Aust
Citation: Biochemistry And Molecular Biology International. Academic Press Aust, v. 42, n. 2, n. 255, n. 260, 1997.
Rights: fechado
Date Issue: 1997
Appears in Collections:Unicamp - Artigos e Outros Documentos

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