Abstract
In the animal kingdom there are four types of O2-binding (respiratory) pigment with different structures but very similar functional properties. They have characteristic colours in their oxygenated states and the absorption spectra of the pigments with bound O2 or another ligand, such as CO or CN−, are used for purposes of identification (Table 7.1). The structures of the binding sites vary (Fig. 7.1): the prosthetic group of the globins is protohaem, i.e. Fe(II)-protoporphyring (Fig. 7.2), which can bind one ligand. Chlorocruorin is also a haemoprotein but with a haem component (spirographis haem) which differs from protohaem in one substituent (Fig. 7.2). In the copper protein haemocyanin and the iron protein haemerythrin, the binding site in each case contains two metal atoms (Fig. 7.1). Chlorocruorins and haemocyanins are always found dissolved in the blood plasma; haemerythrins occur only intracellularly, and haemoglobins are both intra-and extracellular (Table 7.2). The intracellular respiratory pigments consistently have molecular masses under 100 kDA and only one to eight O2-binding sites per molecule. Most of the extracellular blood pigments have far larger molecular masses of up to several million kDA and often more than 100 O2-binding sites; in this way, the colloid osmotic effects in the blood plasma are reduced. There are, however, some exceptions to this rule, e.g. the extracellular haemoglobins of chironomid larvae are only 16–32 kDA.
Access this chapter
Tax calculation will be finalised at checkout
Purchases are for personal use only
Preview
Unable to display preview. Download preview PDF.
References
Abbasi A. and Braunitzer G.: The primary structure of hemoglobins from the domestic cat (Felis catus, Felidae). Biol. Chem. Hoppe-Seyler 366: 699–704 (1985)
Abbasi A. et al.: Molecular basis for ATP/2,3bisphosphoglycerate control switch-over (poikilotherm/homeotherm): An intermediate amino-acid sequence in the hemoglobin of the great Indian rhinoceros (Rhinoceros unicornis, Perissodactyla). Biol. Chem. Hoppe-Seyler 368: 323–332 (1987)
Arents G. and Love W. E.: Glycera dibranchiata hemoglobin. Structure and refinement at 1.5 A resolution. J. mol. Biol. 210: 149–161 (1989)
Aschauer H., Weber R. E. and Braunitzer G.: The primary structure of the hemoglobin of the dogfish shark (Squalus acanthias). Antagonistic effects of ATP and urea on oxygen affinity of an elasmobranch hemoglobin. Biol. Chem. Hoppe-Seyler 366: 589–599 (1985)
Bak H. J. and Beintema J. J.: Panulirus interruptus hemocyanin–The elucidation of the complete amino acid sequence of subunit a. Eur. J. Biochem. 169: 333–348 (1987)
Banville D. and Williams J. G.: The pattern of expression of the Xenopus laevis tadpole a-globin genes and the amino acid sequence of the three major tadpole a-globin polypeptides. Nucleic Acids Res. 13: 5407–21 (1985)
Banville D. and Williams J H.: Developmental changes in the pattern of larval ß-globin gene expression in Xenopus laevis. Identification of two early larval 13-globin mRNA sequences. J. mol. Biol. 184: 611–620 (1985)
Bartlett G. R.: Phosphate compounds in vertebrate red blood cells. Amer. Zool. 20: 103–114 (1980)
Bashford D., Chothia C. and Lesk A. M.: Determinants of a protein fold. Unique features of the globin amino acid sequences. J. mol. Biol. 196: 199–216 (1987)
Bellelli A. et al.: Haem disorder in two myoglobins: comparison of reorientation rate. Biochem. J. 246: 787–789 (1987)
Bieber E. A. and Braunitzer G.: Prae-and perinatal oxygen transport in mammals: The embryonic hemoglobins of the pig (Sus scrofa domestica). Hoppe-Seyler’s Z. physiol. Chem. 365: 321–334 (1984)
Bijlholt M. and van Bruggen E. F. J.: A model for the architecture of the hemocyanin from the arthropod Squilla mantis (Crustacea, Stomatopoda). Eur. J. Biochem. 155: 339–344 (1986)
Biswanger H.: Theorie and Methoden der Enzymkinetik. Verlag Chemie, Weinheim 1979
Blanchetot A., Price M. and Jeffreys A. J.: The mouse myoglobin gene–Characterization and sequence comparison with other mammalian myoglobin genes. Eur. J. Biochem. 159: 469–474 (1986)
Bogusz D. et al.: Functioning haemoglobin genes in non-nodulating plants. Nature 331: 178–180 (1988)
Boisset N. et al.: Three-dimensional reconstruction of native Androctonus australis hemocyanin. J. mol. Biol. 216: 743–760 (1990)
Borgese T. A., Harrington J. P. and Hoffman D.: Anadara ovalis hemoglobins: distinct dissociation and ligand binding characteristics. Comp. Biochem. Physiol. Pt. B. 86: 155–165 (1987)
Borgese T. A. et al.: Haemoglobin properties and polymerization in the marine teleost Lophius americanus (goosefish). Comp. Biochem. Physiol. Pt. B 91: 663–670 (1988)
Braunitzer G. and Hiebl I.: Molecular aspects of high altitude respiration in birds (In German). Naturwissenschaften 75: 280–287 (1988)
Brittain T. and Wells R. M. G.: Characterization of the changes in the state of aggregation induced by ligand binding in the hemoglobin system of a primitive vertebrate, the hagfish Eptatretus cirrhatus. Comp. Biochem. Physiol. Pt. A 85: 785–790 (1986)
Brittain T.: The Root effect. Comp. Biochem. Physiol. Pt. B 86: 473–481 (1987)
Brittain T.: Co-operative functioning of the dimeric haemoglobin obtained from the radular muscle of the amphineurian mollusc Amaurochiton glaucus. Comp. Biochem. Physiol. Pt. B 96: 96–295 (1990)
Brix O.: The adaptive significance of the reversed Bohr and Root shifts in blood from the marine gastropod, Buccinum undatum. J. exp. Zool. 221: 27–36 (1982)
Brix O. et al.: The chloride shift may faciliatate oxygen loading and unloading to/from the hemoglobin from the brown bear (Ursus arctos L.). Comp. Biochem. Physiol. Pt. B 95: 865–868 (1990)
Brouwer M. and Serigstad B.: Allosteric control in Limulus polyphemus hemocyanin: Function relevance of interactions between hexamers. Biochemistry 28: 8819–27 (1989)
Brunori M. et al.: Is there a Root effect in Xenopus hemoglobin? FEBS Letters 221: 161–166 (1987)
Bunn H. F.: Regulation of hemoglobin function in mammals. Amer. Zool. 20: 199–211 (1980)
Bunn H. F. and Forget B. G.: Hemoglobin. Molecular, genetic and clinical aspects. Saunders, Washington 1986
Burnett L. E., Scholnick D. A. and Mangum C. P.: Temperature sensitivity of molluscan and arthropod hemocyanins Biol. Bull. 174: 153–162 (1988)
Cardellini P and Sala M.: Developmental time of the hemoglobin transition in the anuran Bombina orientalis. Comp. Biochem. Physiol. Pt. B 75: 259–262 (1983)
Chacko V. P. et al.: Proton-magnetic-resonance investigation of the dynamics of the conformational transition in allosteric monomeric insect hemoglobins. Eur. J. Biochem. 161: 375–381 (1986)
Cheng, J. E, Krane D. E. and Hardison R. C.: Nucleotide sequence and expression of rabbit globin genes zeta-1, zeta-2 and zeta-3. Pseudogenes generated by block duplications are transcriptionally competent. J. Biol. Chem. 263: 9981–93 (1988)
Cirotto C. and Arangi I.: Koelliker haemoglobins in developing chick embryo. Comp. Biochem. Physiol. Pt. B 92: 103–109 (1989)
Clegg J. B.: Gene conversions in the horse a-globin gene complex. Mol. Biol. Evol. 4: 492–503 (1987)
Colacino J. M. and Kraus D. W.: Hemoglobin-containing cells of Neodasys (Gastrotricha, Chaetonotida)–II. Respiratory significance. Comp. Biochem. Physiol. Pt. A 79: 363–369 (1984)
Coletta M. et al.: Ligand-dependent behaviour of the hemoglobin from the ascarid Parascaris equorum. Biochim. biophys. Acta 870: 169–175 (1986)
Coletta M. et al.: A novel mechanism of heme-heme interaction in the homodimeric hemoglobin from Scapharca inaequivalis as manifested upon cleavage of the proximal Fe-N bond at low pH. J. Biol. Chem. 265: 4828–30 (1990)
Dafré A. L. and F ° D. W.: Root effect hemoglobins in marine fish. Comp. Biochem. Physiol. Pt. A 92: 267–471 (1989)
Darawshe S., Tsafandya Y and Daniel E.: Quaternary structure of erythrocruorin from the nematode Ascaris suum. Evidence for unsaturated haem-binding sites. Biochem. J. 242: 689–694 (1987)
Decker H. and Sterner R.: Nested allostery of arthropodan hemocyanin (Eurypelma californicum and Homarus americanus). J. mol. Biol. 211: 281–293 (1990)
Douglas E. L. et al.: Myoglobin in the heart tissue of fishes lacking hemoglobin. Comp. Biochem. Physiol. Pt. A 81: 885–888 (1985)
Drexel R. et al.: Complete amino-acid sequence of a functional unit from a molluscan hemocyanin (Helix pomatia). Biol. Chem. Hoppe-Seyler 368: 617–635 (1987)
Ellerton H. D., Bearman C. H. and Loong P. C.: Erythrocruorin from the New Zealand earthworm Maoridrilus montanus: a multi-subunit annelid extra-cellular hemoglobin. Comp. Biochem. Physiol. Pt. B 87: 1017–23 (1987)
Fitch D. H. A. et al.: Molecular history of gene conversions in the primate fetal gamma-globin genes. Nucleotide sequences from the common gibbon, Hylobates lar. J. Biol. Chem. 265: 781–793 (1990)
Focesi A. jr., Ogo S. H. and Matsuura M. S. A.: Dimer-tetramer transition in hemoglobins from Liophis miliaris II Evidence with the stripped proteins. Comp. Biochem. Physiol. Pt. B 96: 119–122 (1990)
Garey J. R. and Riggs A. E.: The hemoglobin of Urechis caupo. The cDNA-derived amino acid sequence. J. biol. Chem. 261: 16446–50 (1986)
Garner K. J. and Lingrei J. B.: A comparison of the 13A- and 3B-globin gene clusters of sheep. J. mol. Evol. 28: 175–184 (1989)
Gelissen G., Hennecke R. and Spindler K. D.: The site of synthesis of hemocyanin in the crayfish, Astacus leptodactylus. Experientia 47: 194-/195 (1991)
Giardina B. et al.: Interaction of hemoglobin with chloride and 2,3-bisphophoglycerate: A comparative approach. Eur. J. Biochem. 194: 61–65 (1990)
Gibson Q. H. et al.: Ligand binding in a hierarchy of globin complexes: The hexagonal bilayer hemoglobin of Lumbricus terrestris and its heme-containing subunits. J. Biol. Chem. 266: 13097–102 (1991)
Gielens C. et al.: Identification, separation and characterization of the haemocyanin components of Helix aspersa. Comp. Biochem. Physiol. Pt. B 88: 181–186 (1987)
Gonzalez-Redondo J. M. et al.: Nucleotide sequence of the human theta-1 globin gene. Biochem. Genet. 26: 207–211 (1988)
Goodman M. et al: Amino acid sequence evidence on the phylogeny of primates and other eutherians. In: Goodman M (ed.): Macromolecular sequences in systematics and evolutionary biology, pp. 115–191. Plenum, New York 1982
Goodman M. et al.: The eta-globin gene. Its long evolutionary history in the 13-globin gene family of mammals. J. mol. Biol. 180: 803–823 (1984)
Goodman M. et al.: An evolutionary tree for invertebrate globin sequences. J. mol. Evol. 27: 236–249 (1988)
Gotoh T. and Suzuki T.: Molecular assembly and evolution of multi-subunit extracellular annelid hemoglobins. Zool. Sci. 7: 1–16 (1990)
Grinich N. R, Terwilliger R. C. and Terwilliger N. B.: Oxygen equilibria and structural characteristics of the tetrameric and polymeric intracellular hemoglobins from the bivalve mollusc Barbatia reeveana. J. comp. Physiol. B 156: 675–682 (1986)
Hardison R. C. and Gelinas R. E.: Assignment of orthologous relationships among mammalian aglobin genes by examining flanking regions reveals a rapid rate of evolution. Mol. Biol. Evol. 3: 243–261 (1986)
Hardison R. C. et al.: A previously undetected pseudogen in the human alpha globin gene cluster. Nucleic Acids Res. 14: 1903–11 (1986)
Harris S. et al.: Nucleotide sequence analysis of the lemur 3-globin gene family: Evidence for major rate fluctuations in globin polypeptide evolution. Mol. Biol. Evol. 3: 465–484 (1986)
Herskovits T. T. and Hamilton M. G.: The hemoglobin of the aquatic snail, Planorbella duryi (Wetherby). Comp. Biochem. Physiol. Pt. B 95: 321–326 (1990)
Herskovits T. T. et al: Light-scattering and scanning transmission electron microscopic investigation of the hemocyanin of the bivalve, Yoldia limatula (Say). Comp. Biochem. Physiol. Pt. B 96: 497–503 (1990)
Herskovits T. T. and Hamilton M. G.: Higher order assemblies of molluscan hemocyanins (Minireview). Comp. Biochem. Physiol. Pt. B 99: 19–34 (1991)
Hirsch R. E. and Noble R. W.: Intrinsic fluorescence of carp hemoglobin: a study of the R-T-transition. Biochim. biophys. Acta 914: 213–219 (1987)
Hombrados I. et al.: Primary structure of the minor hemoglobins from the sea lamprey (Petromyzon mar-inns, Cyclostomata). Biol. Chem. Hoppe-Seyler 368: 145–154 (1987)
Honig G. R. and Adams J. G. (eds.): Human hemoglobin genetics. Springer, Wien 1986
Honzatko R. B. and Hendrickson W. A.: Molecular models for the putative dimer of sea lamprey hemoglobin. Proc. Nat. Acad. Sci. USA 83: 8487–91 (1986)
Hsu L. et al.: Structure and expression of the human theta-globin gene. Nature 331: 94–96 (1988)
Huber E. and Brausitzer G.: The primary structure of the hemoglobin of the electric eel (Electrophorus electricus). Biol. Chem. Hoppe-Seyler 370: 245–250 (1989)
Huisman T. H. J.: A comprehensive list of all hemoglobin variants and their references. Hemoglobin 13: 221–323 (1989)
van Iersel A. A. J. and Blaauboer B. J.: NADHferrihemoglobin reductase in avian erythrocytes. Comp. Biochem. Physiol. Pt. B 81: 1027–31 (1985)
di Iorio E. E. et al.: Kinetics of oxygen and carbon monoxide binding to liver fluke (Dicrocoelium dendriticum) hemoglobin. J. biol. Chem. 260: 2160–64 (1985)
Iwaasa H., Takagi T. and Shikama K.: Protozoan hemoglobin from Tetrahymena pyriformis. Isolation, characterization, and amino acid sequence. J. Biol. Chem. 265: 8603–09 (1990)
Jannasch H. W.: Deepsea life on the basis of chemical synthesis (In German). Naturwissenschaften 72: 285–290 (1985)
Jensen E. B. et al.: A three-state MWC analysis of oxygenation in tench (Tina tinca) hemoglobin. J. comp. Physiol. B 160: 407–411 (1990)
Jhiang S. M. and Riggs A. F: The structure of the gene encoding chain c of the hemoglobin of the earthworm, Lumbricus terrestris. J. Biol. Chem. 264: 19003–08 (1989)
Johnson B. A.: Structure and function of the hemocyanin from a semiterrestrial crab, Ocypode quadrata. J. comp. Physiol. B 157: 501–509 (1987)
Jones G. et al.: Molecular cloning, regulation, and complete sequence of a hemocyanin-related, juvenile hormone-suppressible protein from insect hemolymph. J. Biol. Chem. 265: 8596–8602 (1990)
Kapp O. H. et al.: Quaternary structure of the giant extracellular hemoglobin of the leech Macrobdella decora. J. mol. Biol. 213: 141–158 (1990)
Karlson S. and Nienhuis A. W.: Developmental regulation of human globin genes. Annual Rev. Biochem. 54: 1071–1108 (1985)
Kleinschmidt T. and Sgouros J. G.: Hemoglobin sequences. Biol. Chem. Hoppe-Seyler 368: 579–615 (1987)
Kleinschmidt T., Keyl H. G. and Braunitzer G.: Comparison of insect hemoglobins (erythrocruorins) from Chironomus thummi thummi and Chironomus thummi piger (Diptera): The primary stucture of the monomeric hemoglobin CPTIII. Biol. Chem. HoppeSeyler 370: 839–845 (1989)
Klippenstein G. L.: Structural aspects of hemerythrin and myohemerythrin. Amer. Zool. 20: 39–51 (1980)
Knöchel W et al.: Globin evolution in the genus Xenopus: Comparative analysis of cDNAs coding for adult globin polypeptides of Xenopus borealis and Xenopus tropicalis. J. mol. Evol. 23: 211–223 (1986)
Kobayashi M., Nezu T. and Tanaka Y.: Hypoxic induction of hemoglobin synthesis in Daphnia magna. Comp. Biochem. Physiol. Pt. A 97: 513–517 (1990)
Kolatkar P. R. et al.: Novel subunit structure observed for noncooperative hemoglobin from Urechis caupo. J. biol. Chem. 263: 3462–65 (1988)
Komiyama M. H. et al.: Was the loss of the D-helix in a-globin a functional neutral mutation? Nature 352: 349–351 (1991)
Koop B. F. and Goodman M.: Evolutionary and developmental aspects of two hemoglobin 13-chain genes (epsilon-M and beta-M) of opossum. Proc. Nat. Acad. Sci. USA 85: 3893–97 (1988)
Koop B. F. et al.: Tarsius delta-and beta-globin genes: conversions, evolution and systematic implications. J. Biol. Chem. 264: 68–79 (1989)
Kortt A. A., Trinick M. J. and Appleby C A: Amino acid sequences of hemoglobins I and II from root nodules of the non-leguminous Parasponia rigida-Rhizobium symbiosis, and a correction of the sequence of hemoglobin I from Parasponia andersonii. Eur. J. Biochem. 175: 141–149 (1988)
van Kuik J. A. et al.: Primary structure of the neutral carbohydrate chains of hemocyanin from Panulirus interruptus. Eur. J. Biochem. 159: 297–301 (1986)
van Kuik J. A. et al.: Primary structure of the acidic carbohydrate chain of hemocyanin from Panulirus interruptus. FEBS Letters 221: 150–154 (1987)
van Kuik J. A. et al.: Primary structure determination of seven novel N-linked carbohydrate chains derived from hemocyanin of Lymnaea stagnalis–3–0Methyl-D-galactose and N-acetyl-D-galactosamin as constituents of xylose-containing N-linked oligosaccharides in an animal glycoprotein. Eur. J. Biochem. 169: 399–411 (1987)
Lallier E. and Truchot J. P.: Modulation of hemocyainn oxygen affinity by L-lactate and urate in the prawn Penaeus japonicus. J. exp. Biol. 147: 133–146 (1989)
Landsmann J. et al.: Common evolutionary origin of legume and non-legume plant haemoglobins. Nature 324: 166–168 (1986)
Lang W. H.: cDNA cloning of the Octopus dofleini hemocyanin: Sequence of the carboxyl-terminal domain Biochemistry 27: 7276–82 (1988)
Lecomte J. T. J. et al.: Structural and electronic properties of the liver fluke heme cavity by nuclear magnetic resonance and optical spectroscopy. Evidence for a distal tyrosine residue in a normally functioning hemoglobin. J. mol. Biol. 209: 235–247 (1989)
Lee A. W. and Karplus M.: Structure-specific model of hemoglobin cooperativity. Proc. Nat. Acad. Sci. USA 80: 7055–59 (1983)
Leidescher T. and Decker H.: Conformational changes of tarantula (Eurypelma californicum) hemocyanin detected with a fluorescent probe, 7chloro-4-nitrobenzo-2-oxa-1,3-diazole. Eur. J. Biochem. 187: 617–625 (1990)
Lerch K. et al.: Different origins of metal binding sites in binuclear copper proteins, tyrosinase and hemocyanin J inorg. Biochem. 26: 213–217 (1986)
Lesk A. M. and Chothia C.: How different amino acid sequences determine similar protein structures: The structure and evolutionary dynamics of the globins. J. mol. Biol. 136: 225–270 (1980)
Leung S. O., Proudfoot N. J. and Whitelaw E.: The gene for theta-globin is transcribed in human fetal erythroid tissues. Nature 329: 551–554 (1987)
Levy M. J. et al.: Isolation and characterization of methemoglobin reductase from yellowfin tuna (Thun-nus albacares). Comp. Biochem. Physiol. Pt. B 81: 809–814 (1985)
Leyko W. and Osmulski P. A.: Seasonal variability of hemoglobin content and component composition of Chironomus thummi larvae. Comp. Biochem. Physiol. Pt. B 89: 613–616 (1985)
Li Q. L. et al.: Beta-globin locus activation regions. Conservation of organization, structure and function. Proc. Nat. Acad. Sci. USA 87: 8207–11 (1990)
Liebhaber S. A., Cash E E. and Ballas S. K.: Human a-globin gene expression. The dominant role of the a2-locus in mRNA and protein synthesis. J. biol. Chem. 261: 15327–33 (1986)
Lima A. A. B. et al.: Allosteric effect of protons and adenosine triphosphate on hemoglobins from aquatic amphibia. J. comp. Physiol. B 155: 353–355 (1985)
Linzen B. (ed.): Invertebrate oxygen carriers. Springer, Berlin 1986
Linzen B.: Blue blood. Structure and evolution of hemocyanins (In German). Naturwissenschaften 76: 206–211 (1989).
Livingston D. J., Watts D. A. and Brown W. D.: Myoglobin interspecies structural differences: effects on autoxidation and oxygenation. Arch. Biochem. Biophys. 249: 106–115 (1986)
Makino N.: Subunits of Panulirus japonicus hemocyanin. 2. Cooperativity of the homogonous hexamers. Eur. J. Biochem. 173: 431–435 (1988)
Mangum C. P. (ed.): Blood and oxygen carriers. Springer, New York 1992
Manwell C. and Baker C. M. A.: Magelona haemerythrin: tissues specificity, molecular weights and oxygen equilibiria. Comp. Biochem. Physiol. Pt. B 89: 453–463 (1988)
Margot J. B., Demers G. W. and Hardison R. C.: Complete nucleotide sequence of the rabbit 13-like globin gene cluster. J. mol. Biol. 205: 15–40 (1989)
Markl J.: Evolution and function of structurally diverse subunits in the respiratory protein hemocyanin from arthropods. Biol. Bull. 171: 90–115 (1986)
Markl J. et al.: Quaternary and subunit structure of Calliphora arylphorin as deduced from electron microscopy, electrophoresis, and sequence similarities with arthropod hemocyanin. J. comp. Physiol. B 162: 665–680 (1992)
Martin K. D. and Parkhurst L. J.: Kinetics and thermodynamics of oxygen and carbon monoxide binding to the T-state hemoglobin of Urechis caupo. Biochemistry 29: 5718–26 (1990)
Matsuura M. S. A., Fushitani K and Riggs A. E: The amino acid sequences of the a and ß chains of hemoglobin from the snake, Liophis miliaris. J. Biol. Chem. 264: 5515–21 (1989)
Mayr G. W. and Dietrich W.: The only inositol tetrakisphosphate detectable in avian erythrocytes is the isomer lacking phosphate at position 3: a NMR study. FEBS Letters 213: 278–282 (1987)
Miller K. I. and Mangum C. P.: An investigation of the nature of Bohr, Root, and Haldane effects in Octopus dofleini hemocyanin. J. comp. Physiol. B 158: 547–552 (1988)
Miller K. I., Schabtach E. and van Holde K. E.: Arrangement of subunits and domains within the Octopus dofleini hemocyanin. Proc. Nat. Acad. Sci. USA 87: 1496–1500 (1990)
Mintorovitch J., van Pelt D. and Satterlee J. D.: Kinetic study of the slow cyanide binding to Glycera dibranchiata monomer hemoglobin. Biochemistry 28: 6099–6104 (1989)
Miyashita N. et al.: Allelic constitution of the hemoglobin beta chain in wild populations of the house mouse, Mus musculus. Biochem. Genetics 23: 975–986 (1985)
Moon A. M. and Ley T. J.: Conservation of the primary structure, organization, and function of the human and mouse 13-globin locus-activating regions. Proc. Nat. Acad. Sci. USA 87: 7693–97 (1990)
Myers C. R. et al.: Haemoglobin-producing tissue of larvae and pupae of Chironomus thummi (Diptera). J. Insect Physiol. 32: 845–851 (1986)
Nakashima H. et al.: Structure of hemocyanin II from the horseshoe crab, Limulus polyphemus. Sequences of two overlapping peptides, ordering the CNBr fragments, and the complete amino acid sequence. J. biol. Chem. 261: 10526–33 (1986)
Neuteboom B. et al.: Partial amino acid sequence of a hemocyanin subunit from Palinurus vulgaris. Comp. Biochem. Physiol. Pt. B 94: 593–597 (1989)
Osmulski P. A. and Leyko W.: Structure, function and physiological role of Chironomus haemoglobin (Review). Comp. Biochem. Physiol. Pt. B 85: 701–722 (1986)
Padgett R. W. et al.: The molecular organization of the beta-globin complex of the deer mouse, Peromyscus maniculatus. Mol. Biol. Evol. 4: 30–45 (1987)
Peeters K. et al.: The globin composition of Daphnia pulex hemoglobin and the comparison of the amino acid composition of invertebrate hemoglobins. Comp. Biochem. Physiol. Pt. B 97: 369–381 (1990)
Perutz M. F.: Species adaptation in a protein molecule. Mol. Biol. Evol. 1: 1–28 (1983)
Perutz M. E.: Species adaptation in a protein molecule. Adv. Protein Res. 36: 213–244 (1984)
Petruzzelli R. et al.: Amino acid sequence of a-chain of hemoglobin IV from trout (Salmo irideus). Biochim. biophys. Acta 995: 255–258 (1989)
Petruzzelli R. et al.: Scapharca hemoglobins, type cases of a novel mode of chain assembly and hemeheme communication. Amino acid sequence and subunit interactions of the tetrameric. FEBS Letters 259: 133–136)1889)
Powers D. A.: Molecular ecology of teleost fish hemoglobins: strategies for adapting to changing environments. Amer. Zool. 20: 139–162 (1980)
Reischl E. et al.: Bohr effect, electroin spin resonance spectroscopy and subunit dissociation of the hemoglobin components from the turtle Phrynops hilarii. Comp. Biochem. Physiol. Pt. B 78: 251–157 (1984)
Rendell M. et al.: An interspecies comparison of normal levels of glycosylated hemoglobin and glycosylated albumin Comp. Biochem. Physiol. Pt. B 81: 819–822 (1985)
Richardson D. E. et al.: Allosteric interactions in sipunculid and brachiopod hemerythrins. Biochemistry 26: 1003–13 (1987)
Riggs A. F.: The Bohr effect. Annual Rev. Physiol. 50: 181–204 (1988)
Robinson I. B. and Ingram V. M.: Gene evolution in the chicken (3-globin cluster. Cell 28: 515–521 (1982)
Royer W. E. jr., Hendrickson W. A. and Chiancone E.: Structural transitions upon ligand binding in a cooperative dimeric hemoglobin. Science 249: 518–521 (1990)
Rozynek P., Hankeln T. and Schmidt E. R.: Structure of a hemoglobin gene cluster and nucleotide sequence of three hemoglobin genes from the midge Chironomus thummi piger (Diptera, Insecta). Biol. Chem. Hoppe-Seyler 370: 533–542 (1989)
Schartau W. et al.: Hemocyanins in spiders. XIII. Complete amino acid sequence of subunit a Eurypelma californicum. Biol. Chem. Hoppe-Seyler 371: 557–565 (1990)
Schimenti J. C. and Dumcan C. H.: Structure and organization of the bovine 3-globin genes. Mol. Biol. Evol. 2: 514–525 (1985)
Scott E. M. and Harrington J. P.: Methemoglobin reductase activity in fish erythrocytes. Comp. Biochem. Physiol. Pt. B 82: 511–513, (1985)
Shaw J. P., Marks J. and Shen C. K. J.: Evidence that the recently discovered theta-1-globin gene is functional in higher primates. Nature 326: 717–720 (1987)
Shehee W. R. et al.: Nucleotide sequence of the BALB/c mouse 13-globin complex. J. mol. Biol. 205: 41–62 (1989)
Shishikura E et al.: Amino acid sequence of the monomer subunit of the extracellular hemoglobin of Lumbricus terrestris. J. biol. Chem. 262: 3123–31 (1987)
Simpson C. E., Taylor W. J. and Jacobson E. R.: Sickling hemoglobin polymerization in iguana erythrocytes. Comp. Biochem. Physiol. Pt. A 73: 703–708 (1982)
Sizaret P. Y. et al.: A refined quaternary structure of Androctonus australis hemocyanin Eur. J. Biochem. 127: 501–506 (1982)
Smit J. D. G. et al.: Acid Bohr effect of a monomeric haemoglobin from Dicrocoelium dendriticum–Mechanism of the allosteric conformation transition. Eur. J. Biochem. 155: 231–237 (1986)
Stalder J. et al.: Primary structure and evolutionary relationship between the adult a-globin genes and their 5’-flanking regions of Xenopus laevis and Xeno-pus tropicalis. J. mol. Evol. 28: 64–71 (1989)
Standley P. R. et al.: The calcium, copper and zinc content of some annelid extracellular haemoglobins. Biochem. J. 249: 915–916 (1988)
Stern M. S. et al.: Amino acid sequence of the monomer subunit of the giant extracellular hemoglobin of the aquatic oligochaete, Tubifex tubifex. Eur. J. Biochem. 194: 67–73 (1990)
Stoecker W. et al.: The quatenary structure of four crustacean two-hexameric hemocyanins• immunocorrelation, stoichiometry, reassembly and topology of individual subunits. J. comp. Physiol. B 158: 271–289 (1988)
Suzuki T: Amino acid sequence of myoglobin from the mollusc Dolabella auricularia. J. biol. Chem. 261: 3692–99 (1986)
Suzuki T.: Amino acid sequence of a major globin from the sea cucumber Paracaudina chilensis. Biochim. biophys. Acta 998: 292–296 (1989)
Suzuki T. et al.: Hemoglobins from the two closely related clams Barbatia lima and Barbatia virescens. Comparison of their subunit structures and N-terminal sequence of the unusual two-domain chain. Zool. Sci. 6: 269–281 (1989)
Suzuki T., Takagi T. and Ohta S.: Amino acid sequence of the dimeric hemoglobin (Hb I) from the deep-sea cold-seep clam Calyptogena soyoae and the phylogenetic relationship with other molluscan hemoglobins. Biochim. biophys. Acta 999: 254–259 (1989)
Suzuki T., Takagi T. and Gotoh T.: Primary structure of the two linker chains of the extracellular hemoglobin from the polychaete Tylorrhynchus heterochaetus. J. Biol. Chem. 265: 12168–77 (1990)
Suzuki T., Takagi T. and Ohta S.: Primary structure of a constituent polypeptide chain (AIII) of the giant hemoglobin from the deep-sea tube worm Lamellibrachia. A possible hydrogen sulfide-binding site. Biochemistry 266: 221–225 (1990)
Tam L. T., Gray G. P. and Riggs A. E: The hemoglobins of the bullfrog Rana catesbeiana. The structure of the f3-chain of component C and the role of the a-chain in the formation of intermolecular disulfide bonds. J. biol. Chem. 261: 8290–94 (1986)
Terwilliger R. C. and Terwilliger N. B.: Molluscan hemoglobins (Review). Comp. Biochem. Physiol. Pt. B 81: 255–261 (1985)
Terwilliger N. B. et al.: Bivalve hemocyanins–a comparison with other molluscan hemocyanins Comp. Biochem. Physiol. Pt. B 89: 189–195 (1988)
Toulmond A., Jouin C. and de Frescheville J.: Hemocyanin of the protobranch bivalve mollusc Nucula hanleyi Winckworth. Comp. Biochem. Physiol. Pt. B 88: 71–74 (1987)
Trewitt P. M., Boyer D. R. and Bergstrom G.: Characterization of maternal haemoglobin in the eggs and embryos of Chironomus thummi. J. Insect Physiol. 32: 963–969 (1986)
Trotman C. N. A. et al.: The polymeric hemoglobin molecule of Artemia. Interpretation of translated cDNA sequence of nine domains J Biol. Chem. 266: 13789–95 (1991)
Utecht R. E. and Kurtz jr. D. M.: Cytochrome b5 and NADH-cytochrome-b5 reductase from sipunculan erythrocytes; a methemerythrin reduction system from Phascolopsis gouldii. Biochim. biophys. Acta 953: 164–178 (1988)
Val A. L. et al.: Biological aspects of Amazonian fishes–I. Red blood cell phosphates of schooling fishes (genus Semaprochilodus: Prochilodontidae). Comp. Biochem. Physiol. Pt. B 78: 215–217 (1984)
Vandergon T. L. and Colacino J. M.: Characterization of hemoglobin from Phoronis architecta (Phoronida). Comp. Biochem. Physiol. Pt. B 94: 31–39 (1989)
Viana de Freitas T., Alfonso A. M. M. and Neves A. G. A.: Purification and characterization of the glycopeptide II from the hemoglobin of Biomphalaria glabrata. Comp. Biochem. Physiol. Pt. B 81: 743–747 (1985)
Vinson C. R. and Bonaventura J.: Structure and oxygen equilibrium of the three coelomic cell hemoglobins of the echiuran worm Thalassema mellita (Conn). Comp. Biochem. Physiol. Pt. B 87: 361–366 (1987)
Vincent K. A. and Wilson A. C.: Evolution and transcription of Old World monkey globin genes. J. mol. Biol. 207: 465–479 (1989)
Vinogradov S. N. and Kapp O. H. (eds.): Structure and function of invertebrate oxygen carriers. Springer, New York 1991
Vinogradov S. N., Sharma P. K. and Walz D. A.: Iron and heme content of the extracellular hemoglobins and chlorocruorins of annelids (Review). Comp. Biochem. Physiol. Pt. B 98: 187–194 (1991)
Vinogradov S. N. et al.: A dodecamer of globin chains is the principal functioning subunit of the extracellular hemoglobin of Lumbricus terrestris. J. Biol. Chem. 266: 13091–96 (1991)
Voit R. and Feldmaierfuchs G.: Arthropod hemocyanins: Molecular cloning and sequencing of cDNAs encoding the tarantula hemocyanin subunit-A and subunit-E. J. Biol. Chem. 265: 19447–52 (1990)
Volbeda A. and Hol W. G. J.: Crystal structure of hexameric haemocyanin from Panulirus interruptus refined at 3.2 A resolution. J. mol. Biol. 209: 249–279 (1989)
Wache S., Terwilliger N. B. and Terwilliger R. C.: Hemocyanin structure changes during early development of the crab Cancer productus. J. exp. Zool. 247: 23–32 (1988)
Wainwright B. and Hope R.: Cloning and chromosomal location of the a-and ß-globin genes from a marsupial. Proc. Nat. Acad. Sci. USA 82: 8105–08 (1985)
Wakabayashi S., Matsubara H. and Webster D. A.: Primary sequence of a dimeric bacterial haemoglobin from Vitreoscilla. Nature 322: 481–483 (1986)
Weber R. E., Braunitzer G. and Kleinschmidt T.: Functional multiplicity and structural correlations in the hemoglobin system of larvae of Cironomus thummi thummi (Insecta, Diptera): Hb components CTT I, CTT IIß, CTT III, CTT IV, CTT VI, CTT VIIB, CTT IX and CTT X. Comp. Biochem. Physiol. Pt. B 80: 747–753 (1985)
Weber R. E. and Jensen E. B.: Functional adaptations in hemoglobins from ectothermic vertebrates. Annual Rev. Physiol. 50: 161–179 (1988)
Wichertjes T. et al.: The quaternary structure of Sepia officinalis haemocyanin Biochim. biophys. Acta 872: 183–194 (1986)
Willard C. et al.: Comparison of human and chimpanzee zeta-globin genes. J. mol. Evol. 22: 309–315 (1985)
Wills C.: Genetic variability. Clarendon Press, Oxford 1981
Wilson jr. R. R. and Knowles E. C.: Temperature adaptation of fish hemoglobins reflected in rates of autoxidation. Arch. Biochem. Biophys. 255: 210–213 (1987)
Wood E. J. et al.: Relative molecular mass of the polypeptide chain of ßc-haemocyanin of Helix pomatia and carbohydrate composition of the functional units. Comp. Biochem. Physiol. Pt. B 82: 179–186 (1985)
Zafar R. S. et al.: The cDNA sequences encoding two components of the polymeric fraction of the intracellular hemoglobin of Glycera dibranchiata. J. Biol. Chem. 265: 21843–51 (1990)
Zhang K. et al.: The active site of hemerythrin as determined by X-ray absorption fine structure. Biochemistry 27: 7470–79 (1988)
Zimmer J. R. et al.: Kinetic study of the oxygenation process of hemerythrins from Lingula unguis and Siphonosoma crumanense. Biochim. biophys. Acta 874: 174–180 (1986)
Author information
Authors and Affiliations
Rights and permissions
Copyright information
© 1994 Springer-Verlag Berlin Heidelberg
About this chapter
Cite this chapter
Urich, K. (1994). Respiratory Pigments. In: Comparative Animal Biochemistry. Springer, Berlin, Heidelberg. https://doi.org/10.1007/978-3-662-06303-3_7
Download citation
DOI: https://doi.org/10.1007/978-3-662-06303-3_7
Publisher Name: Springer, Berlin, Heidelberg
Print ISBN: 978-3-642-08181-1
Online ISBN: 978-3-662-06303-3
eBook Packages: Springer Book Archive