Comparison of chlorocruorin and annelid hemoglobin quaternary structures.

@article{Terwilliger1976ComparisonOC,
  title={Comparison of chlorocruorin and annelid hemoglobin quaternary structures.},
  author={Robert C. Terwilliger and Nora B. Terwilliger and Eric Schabtach},
  journal={Comparative biochemistry and physiology. A, Comparative physiology},
  year={1976},
  volume={55 1},
  pages={
          51-5
        }
}
Abstract 1. 1. The structures of Eudistylia vancouveri chlorocruorin and Pista pacifica and Thelepus crispus extracellular hemoglobins have been examined by electron microscopy. The intact pigments display a two-tiered hexagonal array characteristic of other annelid high molecular weight hemoglobins and chlorocruorins. 2. 2. The smallest subunit molecular weight of these pigments determined by SDS gel electrophoresis is 14–15,000; Pista hemoglobin contains some additional 30,000 molecular… 
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Abstract The recent measurements of the molecular mass and size of the annelid extracellular hemoglobins and studies of their dissociation in the presence of sodium dodecyl sulfate (SDS) and at
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TLDR
Lamellibrachia hemoglobin closely resembles the extracellular hemoglobins of annelids in many respects but shares the molecular weight heterogeneity previously reported for hemoglobin of R. pachyptila.
Protein and gene structure of a chlorocruorin chain of Eudistylia vancouverii.
TLDR
Based on protein and gene structure it can be concluded that the globin chains of chlorocruorins are not fundamentally different from other annelid Globin chains.
Quaternary structure of the giant extracellular hemoglobin of the leech Macrobdella decora.
TLDR
Three-dimensional reconstruction from microscope images provided a model of Macrobdella hemoglobin that is very similar to the reconstruction of Lumbricus hemoglobin: the radial mass distribution curves are virtually superimposable.
Purification and structure of the polypeptide chains of earthworm hemoglobin.
TLDR
Analysis of chromatography of either globin A or B on carboxymethylcellulose in 8 m urea indicates that three of these bands are unique polypeptides chains, while the fourth, most anodic, band appears to be a product of aggregation and not a uniquepolypeptide chain.
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References

SHOWING 1-10 OF 28 REFERENCES
The structure of annelid and mollusc hemoglobins.
  • L. Waxman
  • Biology, Medicine
    The Journal of biological chemistry
  • 1975
TLDR
The results suggest that several annelid hemoglobins and chlorocruorins have similar structures, and that annelids use small polypeptide chains while molluscs use giantpolypeptides to carry O2.
Quaternary structure of Pista pacifica vascular hemoglobin.
TLDR
The structure and amino acid composition of the vascular hemoglobin of Pista pacifica are compared with hemoglobins of other annelids and with the coelomic cell hemoglOBins of Pistas to demonstrate co-operative oxygen binding similar to that found in the intact polymer.
The hemoglobin of Arenicola cristata.
  • L. Waxman
  • Chemistry, Medicine
    The Journal of biological chemistry
  • 1971
TLDR
Oxygenation studies show that the hemoglobin of the polychaete annelid Arenicola cristata is highly cooperative with a Hill coefficient close to six, but it has a small Bohr effect.
A study of the subunit structure of the extracellular hemoglobin of Lumbricus terrestris.
TLDR
Sodium dodecyl sulfate electrophoresis of Lumbricus hemoglobin in the presence of mercaptoethanol provided a reproducible patterns of six components, four bands with molecular weights of 12,000, 14, thousands, 16,000- and 19,000 - respectively, and two bands with Molecular weights of about 31,000 and 36,000.
The quaternary structura and oxygen equilibrium properties of the vascular hemoglobin of the terebellid polychaete, Thelepus crispus Johnson.
TLDR
The effect of pH and the presence of either Mg2+ or EDTA on oxygen binding and quaternary structure is different from that observed for the vascular hemoglobin of the closely related terebellid polychaete, Pista pacifica.
Molecular weight of Eudistylia vancouveri chlorocruorin and its subunits.
TLDR
The chlorocruorin of the marine polychaete Eudistylia vancouveri has a molecular weight of 3.1-10(6) and a sedimentation coefficient (S020, w) of about 57 S at pH 8.0 whereas in 0l01 M EDTA, the pigment begins to dissociate above pH 9.0 into smaller submultiples.
Coelomic cell hemoglobin of the terebellid polychaete, Thelepus crispus johnson. Structure and oxygen equilibrium.
TLDR
The purified hemoglobin has a pH-independent sigmoid oxygen equilibrium curve with an overall heat of oxygenation of − 8·4 kcal/mole and appears to be homogeneous with respect to ion exchange chromatography and disc gel electrophoresis.
Quaternary structure of Limnodrilus haemoglobin.
TLDR
The results lead to a conclusion that the minimum molecular weight either per haem or per N-terminal residue is approximately 28,000 and the whole molecule consists of about 108 subunits or peptide chains, each containing single haem.
Subunits of Placobdella haemoglobin.
TLDR
The results obtained suggest that Placobdella haemoglobin consists of at least four polypeptide chains possessing molecular weights of approximately 13,000, 15,000), 17,000 and 26,000.
The Amino Acid Sequence of the Monomeric Hemoglobin Component from the Bloodworm, Glycera dibranchiata
TLDR
The complete amino acid sequence of 147 residues has been determined for the major monomeric component of the hemoglobin of the bloodworm, Glycera dibranchiata, and it appears that the distal heme-linked histidine in vertebrate hemoglobins has been replaced by leucine.
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