Amino acid sequence of the monomer subunit of the giant extracellular hemoglobin of the aquatic oligochaete, <i>Tubifex tubifex</i>

Stern, Mary S.; Vinogradov, Serge N.; Sharma, Pawan K.; Ereifej, Khalil; Walz, Daniel A.

doi:10.1111/j.1432-1033.1990.tb19428.x

Cited by 9 publications

(1 citation statement)

References 30 publications

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“…As shown in Table 1, it has been confirmed that T. tubifex can accumulate metals, in line with previous studies (Singh et al 2007). Iron shows the highest level of concentration, and this is strictly correlated with its biological activity inside the giant globins of oligochaetes (Bailly et al 2007;Stern et al 1990). Other metals, as well transition metals and metalloids, are present in the animal tissues with specific range of accumulation, that in the case of Cr reach a ratio of 10^4 with respect to the water where worms live.…”

Section: Metals Quantificationmentioning

confidence: 94%

Environment health and intraspecific biodiversity in T. tubifex: a preliminary analysis of a population from Apennines springs

Spica

Giampaoli

Buggiotti

et al. 2013

Int. J. Environ. Sci. Technol.

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The cosmopolitan freshwater oligochaete Tubifex tubifex is an important health indicator of the aquatic environment. Water pollutants can affect the intraspecific biodiversity grade of local Tubifex colonies. A genetic profile of specimens collected in an environment with reduced anthropic presence is particularly important to define genetic variability in unperturbed Tubifex populations, and it is still missing in the international literature. Therefore, it has been performed the analysis of lineage composition in a T. tubifex colony from high mountain spring ponds in Central Italy, characterized by a very low concentration of heavy metals. The sampling was performed during spring 2010 and 2011, in the Sett'acque valley (1,900 m above mean sea level), within the township of Lucoli. Data presented in this work depicted a peculiar composition of the population, characterized by a reduced complexity compared to other urban environments, and with no specimens belonging to the lineage I, largely described in many European populations. Interestingly, lineage 2e, previously discovered only in a natural reserve, results to be the most common lineage in this population. Considerations on environmental health and genetic evolution are discussed.

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Section: Metals Quantificationmentioning

confidence: 94%

Environment health and intraspecific biodiversity in T. tubifex: a preliminary analysis of a population from Apennines springs

Spica

Giampaoli

Buggiotti

et al. 2013

Int. J. Environ. Sci. Technol.

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Primary structure of the common polypeptide chainb from the multi-hemoglobin system of the hydrothermal vent tube wormRiftia pachyptila: An insight on the sulfide binding-site

et al. 1997

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The deep-sea tube worm Riftia pachyptila Jones possesses a multi-hemoglobin system with three different extracellular Hbs: two dissolved in the vascular blood, V1 (ca. 3,500 kDa) and V2 (ca. 400 kDa), and one in the coelomic fluid, C1 (ca. 400 kDa). V1 Hb consists of four heme-containing, globin chains (b-e) and four linker chains (L1-L4). V2 and C1 Hbs are exclusively built from globin chains, six for V2 (a-f) and five for C1 (a-e). The complete amino acid sequence of the isolated monomeric globin chain b, common to all Riftia Hbs, has been determined by automated Edman degradation sequencing of the peptides derived by digestion with trypsin, chymotrypsin, thermolysin, and CNBr. This polypeptide chain is composed of 144 amino acid residues, providing a M(r) of 16, 135.0 Da. Moreover, the primary sequence of chain b revealed 3 Cys residues at position 4, 75, and 134. Cys-4 and Cys-134 are located at positions where an intra-chain disulfide bridge is formed in all annelid, vestimentiferan, or pogonophoran chains, but Cys-75 is located at a unique position only found in three globin chains belonging to Lamellibrachia and Oligobrachia, a vestimentiferan and a pogonophoran. In both groups, Hbs can bind sulfide reversibly to fuel the chemosynthetic process of the symbiotic bacteria they harbor. Sulfide-binding experiments performed on purified Hb fractions (i.e., V1, V2, and C1 Hbs) suggest that free Cys residues on globin chains, and the numerous Cys found in linker chains, as determined previously by ESI-MS, may be the sulfide binding-sites. Blocking the free Cys by N-ethylmaleimide, we confirmed that free cysteines were involved in sulfide-binding but did not account for the whole sulfide-binding capacity of V1 Hb. Furthermore, a phylogenetic tree was constructed from 18 globin-like chains of annelid, vestimentiferan, and pogonophoran extracellular Hbs to clarify the systematic position of tubeworms. Riftia chain b clearly belongs to the "strain A" family with 30 to 80% identity with the other sequences analyzed. Its position in the tree confirmed a close relationship between vestimentiferan, pogonophoran, and annelid Hbs.

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Respiratory Pigments

Urich

1994

Comparative Animal Biochemistry

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Amino acid sequence of the monomer subunit of the giant extracellular hemoglobin of the aquatic oligochaete, Tubifex tubifex

Cited by 9 publications

References 30 publications

Environment health and intraspecific biodiversity in T. tubifex: a preliminary analysis of a population from Apennines springs

Environment health and intraspecific biodiversity in T. tubifex: a preliminary analysis of a population from Apennines springs

Primary structure of the common polypeptide chainb from the multi-hemoglobin system of the hydrothermal vent tube wormRiftia pachyptila: An insight on the sulfide binding-site

Respiratory Pigments

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