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. 1986 Jan;49(1):173–175.

DISCUSSION

PMCID: PMC1329618

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Selected References

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

  1. Amzel L. M., McKinney M., Narayanan P., Pedersen P. L. Structure of the mitochondrial F1 ATPase at 9-A resolution. Proc Natl Acad Sci U S A. 1982 Oct;79(19):5852–5856. doi: 10.1073/pnas.79.19.5852. [DOI] [PMC free article] [PubMed] [Google Scholar]
  2. Bannister J. V., Bannister W. H., Anastasi A. Isolation, characterization and oxygen equilibrium of an extracellular haemoglobin from Eunice aphroditois (Passas). Biochem J. 1976 Oct 1;159(1):35–42. doi: 10.1042/bj1590035. [DOI] [PMC free article] [PubMed] [Google Scholar]
  3. CASPAR D. L., KLUG A. Physical principles in the construction of regular viruses. Cold Spring Harb Symp Quant Biol. 1962;27:1–24. doi: 10.1101/sqb.1962.027.001.005. [DOI] [PubMed] [Google Scholar]
  4. Chang C. T., Wu C. S., Yang J. T. Circular dichroic analysis of protein conformation: inclusion of the beta-turns. Anal Biochem. 1978 Nov;91(1):13–31. doi: 10.1016/0003-2697(78)90812-6. [DOI] [PubMed] [Google Scholar]
  5. Chiancone E., Brenowitz M., Ascoli F., Bonaventura C., Bonaventura J. Amphitrite ornata erythrocruorin. I. Structural properties and characterization of subunit interactions. Biochim Biophys Acta. 1980 May 29;623(1):146–162. doi: 10.1016/0005-2795(80)90017-3. [DOI] [PubMed] [Google Scholar]
  6. Chiancone E., Vecchini P., Rossi Fanelli M. R., Antonini E. Studies on erythrocruorin. II. Dissociation of earthworm erythrocruorin. J Mol Biol. 1972 Sep 14;70(1):73–84. doi: 10.1016/0022-2836(72)90164-7. [DOI] [PubMed] [Google Scholar]
  7. Crewe A. V., Crewe D. A., Kapp O. H. Inexact three-dimensional reconstruction of a biological macromolecule from a restricted number of projections. Ultramicroscopy. 1984;13(4):365–371. doi: 10.1016/0304-3991(84)90002-0. [DOI] [PubMed] [Google Scholar]
  8. Crewe A. V. High-resolution scanning transmission electron microscopy. Science. 1983 Jul 22;221(4608):325–330. doi: 10.1126/science.6867711. [DOI] [PubMed] [Google Scholar]
  9. 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]
  10. Fisher R. G., Woods N. E., Fuchs H. E., Sweet R. M. Three-dimensional structures of C-phycocyanin and B-phycoerythrin at 5-A resolution. J Biol Chem. 1980 Jun 10;255(11):5082–5089. [PubMed] [Google Scholar]
  11. Fushitani K., Morimoto H., Ochi O. Preparation of the polypeptides of the giant hemoglobin of Travisia japonica in carbon monoxy form. Arch Biochem Biophys. 1982 Oct 15;218(2):540–547. doi: 10.1016/0003-9861(82)90378-2. [DOI] [PubMed] [Google Scholar]
  12. Garlick R. L., Riggs A. F. The amino acid sequence of a major polypeptide chain of earthworm hemoglobin. J Biol Chem. 1982 Aug 10;257(15):9005–9015. [PubMed] [Google Scholar]
  13. Garlick R. L., Riggs A. Purification and structure of the polypeptide chains of earthworm hemoglobin. Arch Biochem Biophys. 1981 May;208(2):563–575. doi: 10.1016/0003-9861(81)90545-2. [DOI] [PubMed] [Google Scholar]
  14. Gay N. J., Walker J. E. The atp operon: nucleotide sequence of the promoter and the genes for the membrane proteins, and the delta subunit of Escherichia coli ATP-synthase. Nucleic Acids Res. 1981 Aug 25;9(16):3919–3926. doi: 10.1093/nar/9.16.3919. [DOI] [PMC free article] [PubMed] [Google Scholar]
  15. Greer J. Model for haptoglobin heavy chain based upon structural homology. Proc Natl Acad Sci U S A. 1980 Jun;77(6):3393–3397. doi: 10.1073/pnas.77.6.3393. [DOI] [PMC free article] [PubMed] [Google Scholar]
  16. 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]
  17. 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]
  18. Harrison S. C. Protein interfaces and intersubunit bonding. The case of tomato bushy stunt virus. Biophys J. 1980 Oct;32(1):139–153. doi: 10.1016/S0006-3495(80)84930-7. [DOI] [PMC free article] [PubMed] [Google Scholar]
  19. Kam Z., Borochov N., Eisenberg H. Dependence of laser light scattering of DNA on NaCl concentration. Biopolymers. 1981 Dec;20(12):2671–2690. doi: 10.1002/bip.1981.360201213. [DOI] [PubMed] [Google Scholar]
  20. Kapp O. H., Polidori G., Mainwaring M. G., Crewe A. V., Vinogradov S. N. The reassociation of Lumbricus terrestris hemoglobin dissociated at alkaline pH. J Biol Chem. 1984 Jan 10;259(1):628–639. [PubMed] [Google Scholar]
  21. Karlin A., Holtzman E., Yodh N., Lobel P., Wall J., Hainfeld J. The arrangement of the subunits of the acetylcholine receptor of Torpedo californica. J Biol Chem. 1983 Jun 10;258(11):6678–6681. [PubMed] [Google Scholar]
  22. Klug A. Architectural design of spherical viruses. Nature. 1983 Jun 2;303(5916):378–379. doi: 10.1038/303378a0. [DOI] [PubMed] [Google Scholar]
  23. 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]
  24. Lamy J., Bijlholt M. C., Sizaret P. Y., Lamy J., van Bruggen E. F. Quaternary structure of scorpion (Androctonus australis) hemocyanin. Localization of subunits with immunological methods and electron microscopy. Biochemistry. 1981 Mar 31;20(7):1849–1856. doi: 10.1021/bi00510a021. [DOI] [PubMed] [Google Scholar]
  25. Lamy J., Lamy J., Billiald P., Sizaret P. Y., Cavé G., Frank J., Motta G. Approach to the direct intramolecular localization of antigenic determinants in Androctonus australis hemocyanin with monoclonal antibodies by molecular immunoelectron microscopy. Biochemistry. 1985 Sep 24;24(20):5532–5542. doi: 10.1021/bi00341a038. [DOI] [PubMed] [Google Scholar]
  26. Linzen B., Soeter N. M., Riggs A. F., Schneider H. J., Schartau W., Moore M. D., Yokota E., Behrens P. Q., Nakashima H., Takagi T. The structure of arthropod hemocyanins. Science. 1985 Aug 9;229(4713):519–524. doi: 10.1126/science.4023698. [DOI] [PubMed] [Google Scholar]
  27. MONOD J., WYMAN J., CHANGEUX J. P. ON THE NATURE OF ALLOSTERIC TRANSITIONS: A PLAUSIBLE MODEL. J Mol Biol. 1965 May;12:88–118. doi: 10.1016/s0022-2836(65)80285-6. [DOI] [PubMed] [Google Scholar]
  28. Mao D., Wachter E., Wallace B. A. Folding of the mitochondrial proton adenosinetriphosphatase proteolipid channel in phospholipid vesicles. Biochemistry. 1982 Sep 28;21(20):4960–4968. doi: 10.1021/bi00263a020. [DOI] [PubMed] [Google Scholar]
  29. Matthews B. W., Bernhard S. A. Structure and symmetry of oligomeric enzymes. Annu Rev Biophys Bioeng. 1973;2:257–317. doi: 10.1146/annurev.bb.02.060173.001353. [DOI] [PubMed] [Google Scholar]
  30. Noda M., Takahashi H., Tanabe T., Toyosato M., Kikyotani S., Hirose T., Asai M., Takashima H., Inayama S., Miyata T. Primary structures of beta- and delta-subunit precursors of Torpedo californica acetylcholine receptor deduced from cDNA sequences. Nature. 1983 Jan 20;301(5897):251–255. doi: 10.1038/301251a0. [DOI] [PubMed] [Google Scholar]
  31. ROCHE J., BESSIS M., THIERY J. P. [Study of the plasmatic hemoglobin of some Annelidae with the electron microscope]. Biochim Biophys Acta. 1960 Jun 17;41:182–184. doi: 10.1016/0006-3002(60)90397-8. [DOI] [PubMed] [Google Scholar]
  32. Rayment I., Baker T. S., Caspar D. L., Murakami W. T. Polyoma virus capsid structure at 22.5 A resolution. Nature. 1982 Jan 14;295(5845):110–115. doi: 10.1038/295110a0. [DOI] [PMC free article] [PubMed] [Google Scholar]
  33. 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]
  34. Santucci R., Chiancone E., Giardina B. Oxygen binding to Octolasium complanatum erythrocruorin. Modulation of homo- and heterotropic interactions by cations. J Mol Biol. 1984 Nov 15;179(4):713–727. doi: 10.1016/0022-2836(84)90163-3. [DOI] [PubMed] [Google Scholar]
  35. Sato M., Leimbach G., Schwarz W. H., Pollard T. D. Mechanical properties of actin. J Biol Chem. 1985 Jul 15;260(14):8585–8592. [PubMed] [Google Scholar]
  36. Schirmer T., Bode W., Huber R., Sidler W., Zuber H. X-ray crystallographic structure of the light-harvesting biliprotein C-phycocyanin from the thermophilic cyanobacterium Mastigocladus laminosus and its resemblance to globin structures. J Mol Biol. 1985 Jul 20;184(2):257–277. doi: 10.1016/0022-2836(85)90379-1. [DOI] [PubMed] [Google Scholar]
  37. 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]
  38. Suzuki T., Furukohri T., Gotoh T. Subunit structure of extracellular hemoglobin from the polychaete Tylorrhynchus heterochaetus and amino acid sequence of the constituent polypeptide chain (IIC). J Biol Chem. 1985 Mar 10;260(5):3145–3154. [PubMed] [Google Scholar]
  39. 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]
  40. Waxman L. The hemoglobin of Arenicola cristata. J Biol Chem. 1971 Dec 10;246(23):7318–7327. [PubMed] [Google Scholar]
  41. 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]
  42. Wood E. J., Mosby L. J., Robinson M. S. Characterization of the extracellular haemoglobin of Haemopsis sanguisuga (L.). Biochem J. 1976 Mar 1;153(3):589–596. doi: 10.1042/bj1530589. [DOI] [PMC free article] [PubMed] [Google Scholar]
  43. Yu M. H., Glazer A. N. Cyanobacterial phycobilisomes. Role of the linker polypeptides in the assembly of phycocyanin. J Biol Chem. 1982 Apr 10;257(7):3429–3433. [PubMed] [Google Scholar]
  44. van Holde K. E., Miller K. I. Haemocyanins. Q Rev Biophys. 1982 Feb;15(1):1–129. doi: 10.1017/s0033583500002705. [DOI] [PubMed] [Google Scholar]

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