Subunit homology in invertebrate hemoglobins: A primitive heme binding chain?

Vinogradov, Serge N.; Hall, Blanche C.; Shlom, Jerald M.

doi:10.1016/0305-0491(76)90103-6

Cited by 4 publications

(2 citation statements)

References 16 publications

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“…The subunit structure of Pheretimu hemoglobin was examined by SDS/PAGE, and was found mainly to consist of two types of heme-containing subunits; a monomer (chain I) and a disulfide-bonded trimer of chains 11, I11 and IV. This subunit structure is the same as reported in Lumhricus and Tylorrhynchus hemoglobins [3,4], indicating that such a subunit structure is widely conserved in annelid giant hemoglobins. Suzuki and Gotoh [20] proposed a symmetrical 192-chain model for the molecular assembly of Tylorrhynchus hemoglobin, in which the minimum structural entity is a tetramer consisting of the monomer and disulfide-bonded trimer, and the whole molecule is composed of 48 tetramers.…”

Section: Discussionsupporting

confidence: 84%

Amino acid sequence of the monomer subunit of the giant multisubunit hemoglobin from the earthworm Pheretima sieboldi

Suzuki¹

1989

European Journal of Biochemistry

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The giant extracellular hemoglobin of the earthworm Pheretima sieboldi is mainly composed of two hemecontaining subunits: a monomer; chain I and a disulfide‐bonded trimer of chains II, III and IV. Both subunits can be separated easily by gel filtration under alkaline conditions. The amino acid sequence of chain I has been determined. It is composed of 141 residues, has two half‐cystine residues forming a intrachain disulfide bridge, and has a molecular mass of 16911 Da including a heme group. Heterogeneity was found at position 37 (His or Ser). The amino acid sequence of Pheretima chain I showed 30–50% identity with those of eight heme‐containing chains of Lumbricus and Tylorrhynchus hemoglobins. The sequences of nine chains of annelid giant hemoglobins were comparéd separately in the functionally essential central exonic region and structurally essential side exonic regions, and a phylogenetic tree was constructed. The amino acid substitution rate for the central exon was found to be about 1.5 times slower than that for the side exons.

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Section: Discussionsupporting

confidence: 84%

Amino acid sequence of the monomer subunit of the giant multisubunit hemoglobin from the earthworm Pheretima sieboldi

Suzuki¹

1989

European Journal of Biochemistry

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“…As shown in the present work, these proteins are in fact glycoproteins, and there is therefore some uncertainty in the molecular weights as determined by detergent/gel electrophoresis. It is more difficult to account for the finding of Vinogradov et al (1976) that the 12000mol.wt. subunit which they isolated by gel filtration at pH9 contained 0.53 % iron, that is to say one haem group in a mol.wt.…”

Section: Discussionmentioning

confidence: 99%

Isolation, characterization and oxygen equilibrium of an extracellular haemoglobin from Eunice aphroditois (Pallas)

Bannister¹,

Bannister²,

Ánastasi³

1976

Biochemical Journal

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The extracellular haemoglobin from the polychaeta,Eunice aphroditois, existed as a mixture of a heavy major component (so20, w = 56.96 +/- 0.125) and a light minor component (so20, w = 10.00 +/- 0.13S), the latter probably being a dissociation product of the former. The molecular weight of the purified heavier component, as detetermined by sedimentation equilibrium, was 3.44 x 10(6) +/- 0.04x10(6). The molecule had the electron-microscopic appearance typical of annelid haemoglobins, consisting of a stack of two hexagonal plates, with dimensions 26.32 +/- 0.27 nm across the flats of the hexagon, height of stack 17.86 +/- 0.34 nm. The sugar composition is reported, and the isoelectric point was approx. pH7.8. The haem content was 2.31 +/- 0.01%, corresponding to a minimal mol.wt. of 26700. Detergent/gel electrophoresis revealed the presence of at least four bands with molecular weights in the range 14600-31000. Five N-terminal amino acids were found. In addition to the 10S component, which co-existed with the 57S component at all pH values in the range 4.0-10.6, at low pH values (less than pH.5.0) A 16S and a 1.9 S component were found. The absorption and circular-dichroic spectra are reported, and the alpha-helical content, calculated from the ellipticity at 222 nm, was about 40%. The molecule bound O2 co-operatively with a maximum value of the Hill coefficient, h, of 3.9. Over the pH range 7.0-8.0 there was a positive Bohr effect.

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The Oxygenation of Hemoglobin in Lugworms

Mangum¹

1976

Physiological Zoology

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Subunit homology in invertebrate hemoglobins: A primitive heme binding chain?

Cited by 4 publications

References 16 publications

Amino acid sequence of the monomer subunit of the giant multisubunit hemoglobin from the earthworm Pheretima sieboldi

Amino acid sequence of the monomer subunit of the giant multisubunit hemoglobin from the earthworm Pheretima sieboldi

Isolation, characterization and oxygen equilibrium of an extracellular haemoglobin from Eunice aphroditois (Pallas)

The Oxygenation of Hemoglobin in Lugworms

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