The amino acid sequence and oxygen-binding properties of single hemoglobin of the cold-adapted Antarctic teleost Gymnodraco acuticeps

Sapienza University of Rome, Roma, Latium, Italy
Archives of Biochemistry and Biophysics (Impact Factor: 3.02). 02/1992; 292(1):295-302. DOI: 10.1016/0003-9861(92)90082-8
Source: PubMed


The complete amino acid sequence of the single hemoglobin of the Antarctic teleost Gymnodraco acuticeps has been determined. The alpha chain contains 142 amino acid residues; an acetylated seryl residue is at the amino terminal. The beta chain contains 146 residues. A very high degree of sequence identity has been found with hemoglobins of other Antarctic fishes. Oxygen binding is not modulated by pH and allosteric effectors. The Bohr and Root effects are absent, although specific amino acid residues, considered responsible of most of these functions, are conserved in the sequence, thus posing new questions about the molecular basis of these mechanisms. The low heat of oxygenation may be interpreted as one of the mechanisms involved in the process of cold adaptation.

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    • "In detail, alkylation of thiol groups with 4-vinylpyridine and deacylation of the a-chain N terminus were carried out as described previously (D'Avino & di Prisco, 1989; Tamburrini et al., 1992, 1996). Alkylated globins were purified by reverse-phase HPLC, on a C4 Vydac column (4.6 9 250 mm). "
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    ABSTRACT: This study addresses the primary structure, the oxygen-binding properties and the CO-rebinding kinetics of the haemoglobins of the Patagonian toothfish Dissostichus eleginoides. D. eleginoides belongs to the family Nototheniidae, the most diversified of the suborder Notothenioidei, mostly exhibiting an Antarctic distribution. Some of its features are typical of Antarctic species, some are not. For instance, D. eleginoides appears not to have functional antifreeze glycoproteins (consistent with its non-Antarctic distribution). In contrast, it has a major and a minor haemoglobin (similar to many Antarctic notothenioids), and their very low oxygen affinity does not follow the trend of other non-Antarctic notothenioids and appears typical of cold-adapted species. Moreover, the amino-acid sequence reveals high identity with the globins of Antarctic notothenioids, arguing in favour of a common origin within notothenioids, and indicates that the primary structure of the major and minor haemoglobins has undergone modifications only to a limited extent. The ligand-rebinding kinetics of the major haemoglobin of D. eleginoides indicate a strong stabilisation of the quaternary T state at lower pH values.
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    • "Fish constitute more than 23,000 species and live in wide range of environments (Helfman et al. 1997) and fish hemoglobins have shown a huge variation in components and oxygen-binding mechanisms (Weber 1982, 1996). For example, Tamburrini et al. (1992) studied the Antarctic fish hemoglobin and found that Gymnodraco acuticeps has a single hemoglobin without the Bohr effect, indicating that the role of this "
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    ABSTRACT: Cathepsin S is a lysosomal cysteine endopeptidase of the papain family. Our preliminary results showed the up-regulation of cathepsin S (CTSS) transcript during the early stage of Edwardsiella ictaluri infection, leading us to speculate that CTSS may play a role in infection. In this report, we identified, sequenced and characterized the channel catfish CTSS cDNA. Total RNA from tissues was isolated and cDNA libraries were constructed by the rapid amplification cDNA end (RACE) method. The gene-specific primers in conjunction with the RACE primers were used to PCR amplify 5'- and 3'-ends of the CTSS transcript. The complete channel catfish CTSS cDNA comprised 1530 nucleotides including a 96-nucleotide 5'-untranslated region (UTR), a 990-nucleotide open reading frame and a 444-nucleotide 3'-UTR. The open reading frame appears to encode a protein of 329 amino-acid residues with calculated molecular mass of 36.7kDa and pI of 5.96. The degree of conservation of the channel catfish CTSS amino-acid sequence in comparison to other species ranged from 56.6 to 68.5%. These results provide important information for further exploring the roles of channel catfish CTSS in antigen processing.
    Preview · Article · Sep 2008 · Veterinary Immunology and Immunopathology
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    • "The hydrolysate is suspended in 0.1% TFA and clarified by centrifugation. Separation of tryptic peptides (Tamburrini et al., 1992) is carried out by HPLC on a m-Bondapack C 18 reverse-phase column equilibrated with 0.1% TFA in water (solvent A) and 0.08% TFA in 99.92% acetonitrile (solvent B). Elution is carried out at a flow rate of 1 ml/min, and the eluate is monitored by measuring the absorbance at 220 and 280 nm. "
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