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. 1975 Aug;149(2):437–445. doi: 10.1042/bj1490437

Physicochemical properties of Planorbis corneus erythrocruorin.

E J Wood, L J Mosby
PMCID: PMC1165637  PMID: 1180905

Abstract

The erythrocruorin from the snail Planorbis corneus had a sedimentation coefficient, so/20,w, of 33.5 +/- 0.31 S, and a molecular weight of 1.65 x 10(6) +/- 0.04 x 10(6) by high-speed sedimentation-equilibrium ultracentrifugation. The amino acid composition and absorption spectrum of the protein are reported. A very low number of half-cystine residues was found, corresponding to 0.4 residue per haem group. The haem content was 2.76 +/- 0.22%, corresponding to a protein molecular weight of about 22300. Under both acid and alkaline conditions partial dissociation took place to yield mixtures of products that could not be identified. A subunit corresponding to that containing one haem group was not obtained under any of the dossociating conditions tried. Electron microscopy revealed a ring-shaped molecule about 12.2 +/- 0.5 nm in diameter. The native erythrocruorin bound O2 co-operatively, the intermediate value of h in Hill plots having values between 1.7 and 3.4 depending on the conditions.

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

  1. Almeida A. P., Neves A. G. The hemoglobin of Biomphalaria glabrata: chemical composition and some physicochemical properties. Biochim Biophys Acta. 1974 Nov 5;371(1):140–146. doi: 10.1016/0005-2795(74)90162-7. [DOI] [PubMed] [Google Scholar]
  2. Bannister J., Bannister W., Wood E. Bovine erythrocyte cupro-zinc protein. 1. Isolation and general characterization. Eur J Biochem. 1971 Jan;18(2):178–186. doi: 10.1111/j.1432-1033.1971.tb01228.x. [DOI] [PubMed] [Google Scholar]
  3. Bannister W. H., Wood E. J. Isoelectric focussing and acrylamide gel electrophoresis of human erythrocuprein. Life Sci. 1970 Feb 22;9(4):229–233. doi: 10.1016/0024-3205(70)90229-8. [DOI] [PubMed] [Google Scholar]
  4. Brouwer M., Kuiper H. A. Molecular-weight analysis of Helix pomatia alpha-hemocyanin in guanidine hydrochloride, urea and sodium dodecylsulfate. Eur J Biochem. 1973 Jun 15;35(3):428–435. doi: 10.1111/j.1432-1033.1973.tb02855.x. [DOI] [PubMed] [Google Scholar]
  5. CHEW M. Y., SCUTT P. B., OLIVER I. T., LUGG J. W. ERYTHROCRUORIN OF MARPHYSA SANGUINEA. Biochem J. 1965 Feb;94:378–383. doi: 10.1042/bj0940378. [DOI] [PMC free article] [PubMed] [Google Scholar]
  6. David M. M., Daniel E. Subunit structure of earthworm erythrocruorin. J Mol Biol. 1974 Jul 25;87(1):89–101. doi: 10.1016/0022-2836(74)90561-0. [DOI] [PubMed] [Google Scholar]
  7. FANELLI A. R., ANTONINI E., CAPUTO A. Studies on the structure of hemoglobin. I. Physicochemical properties of human globin. Biochim Biophys Acta. 1958 Dec;30(3):608–615. doi: 10.1016/0006-3002(58)90108-2. [DOI] [PubMed] [Google Scholar]
  8. Fernández-Morán H., van Bruggen E. F., Ohtsuki M. Macromolecular organization of hemocyanins and apohemocyanins as revealed by electron microscopy. J Mol Biol. 1966 Mar;16(1):191–207. doi: 10.1016/s0022-2836(66)80272-3. [DOI] [PubMed] [Google Scholar]
  9. Guerritore D., Bonacci M. L., Brunori M., Antonini E., Wyman J., Rossi-Fanelli A. Studies on chlorocruorin. 3. Electron microscope observations on Spirographis chlorocruorin. J Mol Biol. 1965 Aug;13(1):234–237. doi: 10.1016/s0022-2836(65)80092-4. [DOI] [PubMed] [Google Scholar]
  10. Harrington J. P., Pandolfelli E. R., Herskovits T. T. Solution studies on heme proteins: circular dichroism and optical rotation of Lumbricus terrestris and Glycera dibranchiata hemoglobin. Biochim Biophys Acta. 1973 Nov 11;328(1):61–73. doi: 10.1016/0005-2795(73)90330-9. [DOI] [PubMed] [Google Scholar]
  11. LEVIN O. Electron microscope observations on some 60 s erythrocruorins and their split products. J Mol Biol. 1963 Jan;6:95–101. doi: 10.1016/s0022-2836(63)80084-4. [DOI] [PubMed] [Google Scholar]
  12. Pearson J. S., Wood E. J. Oxygen binding properties of Colus gracilis haemocyanin and its subunits. FEBS Lett. 1974 Nov 15;48(2):246–249. doi: 10.1016/0014-5793(74)80478-3. [DOI] [PubMed] [Google Scholar]
  13. Rossi Fanelli M. R., Chiancone E., Vecchini P., Antonini E. Studies on erythrocruorin. I. Physicochemical properties of earthworm erythrocruorin. Arch Biochem Biophys. 1970 Nov;141(1):278–283. doi: 10.1016/0003-9861(70)90133-5. [DOI] [PubMed] [Google Scholar]
  14. Shlom J. M., Vinogradov S. N. A study of the subunit structure of the extracellular hemoglobin of Lumbricus terrestris. J Biol Chem. 1973 Nov 25;248(22):7904–7912. [PubMed] [Google Scholar]
  15. Swaney J. B., Klotz I. M. Properties of erythrocruorin from Cirraformia grandis. Arch Biochem Biophys. 1971 Dec;147(2):475–486. doi: 10.1016/0003-9861(71)90404-8. [DOI] [PubMed] [Google Scholar]
  16. TEALE F. W. Cleavage of the haem-protein link by acid methylethylketone. Biochim Biophys Acta. 1959 Oct;35:543–543. doi: 10.1016/0006-3002(59)90407-x. [DOI] [PubMed] [Google Scholar]
  17. WYMAN J., Jr LINKED FUNCTIONS AND RECIPROCAL EFFECTS IN HEMOGLOBIN: A SECOND LOOK. Adv Protein Chem. 1964;19:223–286. doi: 10.1016/s0065-3233(08)60190-4. [DOI] [PubMed] [Google Scholar]
  18. Waxman L. The hemoglobin of Arenicola cristata. J Biol Chem. 1971 Dec 10;246(23):7318–7327. [PubMed] [Google Scholar]
  19. Wiechelman K. J., Parkhurst L. J. Kinetics of ligand binding in the hemoglobin of Lumbricus terrestris. Biochemistry. 1972 Nov 21;11(24):4515–4520. doi: 10.1021/bi00774a013. [DOI] [PubMed] [Google Scholar]
  20. YPHANTIS D. A. EQUILIBRIUM ULTRACENTRIFUGATION OF DILUTE SOLUTIONS. Biochemistry. 1964 Mar;3:297–317. doi: 10.1021/bi00891a003. [DOI] [PubMed] [Google Scholar]
  21. ZAAIJER J. J., WOLVEKAMP H. P. Some experiments on the haemoglobin-oxygen equilibrium in the blood of the ramshorn (Planorbis corneus L). Acta Physiol Pharmacol Neerl. 1958 Mar;7(1):56–77. [PubMed] [Google Scholar]
  22. van Bruggen E. F., Weber R. E. Erythrocruorin with anomalous quaternary structure from the polychaete Oenone fulgida. Biochim Biophys Acta. 1974 Jul 7;359(1):210–214. doi: 10.1016/0005-2795(74)90145-7. [DOI] [PubMed] [Google Scholar]
  23. van Driel R., van Bruggen E. F. Oxygen-linked association-dissociation of Helix pomatia hemocyanin. Biochemistry. 1974 Sep 24;13(20):4079–4083. doi: 10.1021/bi00717a003. [DOI] [PubMed] [Google Scholar]

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