282
7 Respiratory Pigments
only at high O2 saturation levels; the Bohr effect
is very small ( References
1. Abbasi A and Braunitzer G.: The primary structure
of hemoglobins from the domestic cat (Felis catus,
Felidae). BioI. Chern. Hoppe-Seyler 366: 699-704
(1985)
2. Abbasi A. et al.: Molecular basis for ATP/2,3bisphosphoglycerate control switch-over (poikilothermlhomeotherm): An intermediate amino-acid
sequence in the hemoglobin of the great Indian rhinoceros (Rhinoceros unicornis, Perissodactyla). BioI.
Chern. Hoppe-Seyler 368: 323-332 (1987)
3. Arents G. and Love W. E.: Glycera dibranchiata
hemoglobin. Structure and refinement at 1.5 A
resolution. J. mol. BioI. 210: 149-161 (1989)
4. 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. BioI. Chern. Hoppe-Seyler 366:
589-599 (1985)
5. 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)
6. 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)
7. Banville D. and Williams J. H.: Developmental
changes in the pattern of larval ~-globin gene expression in Xenopus laevis. Identification of two early larval l3-globin mRNA sequences. J. mol. BioI. 184:
611-620 (1985)
8. Bartlett G. R.: Phosphate compounds in vertebrate
red blood cells. Amer. ZooI. 20: 103-114 (1980)
9. Bashford D., Chothia C. and Lesk A M.: Determinants of a protein fold. Unique features of the globin
amino acid sequences. J. mol. BioI. 196: 199-216
(1987)
10. Bellelli A et al.: Haem disorder in two myoglobins:
comparison of reorientation rate. Biochem. J. 246:
787-789 (1987)
11. 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. physioI. Chern. 365: 321-334
(1984)
12. BijIholt M. and van Bruggen E. E J.: A model for the
architecture of the hemocyanin from the arthropod
Squilla mantis (Crustacea, Stomatopoda). Eur. J.
Biochem. 155: 339-344 (1986)
13. Biswanger H.: Theorie und Methoden der Enzymkinetik. Verlag Chemie, Weinheim 1979
14. 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)
15. Bogusz D. et al.: Functioning haemoglobin genes in
non-nodulating plants. Nature 331: 178-180 (1988)
16. Boisset N. et al.: Three-dimensional reconstruction of
native Androctonus australis hemocyanin. J. mol.
BioI. 216: 743-760 (1990)
17. Borgese T. A, Harrington J. P. and Hoffman D.:
Anadara ovalis hemoglobins: distinct dissociation and
ligand binding characteristics. Compo Biochem. PhysioI. Pt. B. 86: 155-165 (1987)
18. Borgese T. A et al.: Haemoglobin properties and
polymerization in the marine teleost Lophius americanus (goosefish). Compo Biochem. PhysioI. Pt. B
91: 663-670 (1988)
19. Braunitzer G. and Hiebll.: Molecular aspects of high
altitude respiration in birds (In German). Naturwissenschaften 75: 280-287 (1988)
20. 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.
Compo Biochem. PhysioI. Pt. A 85: 785-790 (1986)
21. Brittain T.: The Root effect. Compo Biochem. Physiol. Pt. B 86: 473-481 (1987)
22. Brittain T.: Co-operative functioning of the dimeric
haemoglobin obtained from the radular muscle of the
amphineurian mollusc Amaurochiton glaucus. Compo
Biochem. Physiol. Pt. B 96: 96-295 (1990)
23. Brix 0.: The adaptive significance of the reversed
Bohr and Root shifts in blood from the marine gastropod, Buccinum undatum. J. expo Zool. 221: 27-36
(1982)
24. Brix O. et al.: The chloride shift may faciliatate oxygen loading and unloading to/from the hemoglobin
from the brown bear (Ursus arctos L.). Compo Biochern. Physiol. Pt. B 95: 865-868 (1990)
25. Brouwer M. and Serigstad B.: Allosteric control in
Limulus polyphemus hemocyanin: Function relevance of interactions between hexamers. Biochemistry 28: 8819-27 (1989)
26. Brunori M. et al.: Is there a Root effect in Xenopus
hemoglobin? FEBS Letters 221: 161-166 (1987)
27. Bunn H. E: Regulation of hemoglobin function in
mammals. Amer. Zool. 20: 199-211 (1980)
28. Bunn H. E and Forget B. G.: Hemoglobin. Molecular, genetic and clinical aspects. Saunders, Washington 1986
29. Burnett L. E., Scholnick D. A and Mangum C. P.:
Temperature sensitivity of molluscan and arthropod
hemocyanins. BioI. Bull. 174: 153-162 (1988)
30. Cardellini P and Sala M.: Developmental time of the
hemoglobin transition in the anuran Bombina orientalis. Compo Biochem. Physiol. Pt. B 75: 259-262
(1983)
31. 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)
32. Cheng, J. E, Krane D. E. and Hardison R. c.: Nucleotide sequence and expression of rabbit globin
genes zeta-I, zeta-2 and zeta-3. Pseudogenes generated by block duplications are transcriptionally competent. J. BioI. Chern. 263: 9981-93 (1988)
33. Cirotto C. and Arangi I.: Koelliker haemoglobins in
developing chick embryo. Compo Biochem. PhysioI.
Pt. B 92: 103-109 (1989)
34. Clegg J. B.: Gene conversions in the horse a-globin
gene complex. Mol. BioI. EvoI. 4: 492-503 (1987)
7 Respiratory Pigments
only at high O2 saturation levels; the Bohr effect
is very small ( References
1. Abbasi A and Braunitzer G.: The primary structure
of hemoglobins from the domestic cat (Felis catus,
Felidae). BioI. Chern. Hoppe-Seyler 366: 699-704
(1985)
2. Abbasi A. et al.: Molecular basis for ATP/2,3bisphosphoglycerate control switch-over (poikilothermlhomeotherm): An intermediate amino-acid
sequence in the hemoglobin of the great Indian rhinoceros (Rhinoceros unicornis, Perissodactyla). BioI.
Chern. Hoppe-Seyler 368: 323-332 (1987)
3. Arents G. and Love W. E.: Glycera dibranchiata
hemoglobin. Structure and refinement at 1.5 A
resolution. J. mol. BioI. 210: 149-161 (1989)
4. 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. BioI. Chern. Hoppe-Seyler 366:
589-599 (1985)
5. 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)
6. 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)
7. Banville D. and Williams J. H.: Developmental
changes in the pattern of larval ~-globin gene expression in Xenopus laevis. Identification of two early larval l3-globin mRNA sequences. J. mol. BioI. 184:
611-620 (1985)
8. Bartlett G. R.: Phosphate compounds in vertebrate
red blood cells. Amer. ZooI. 20: 103-114 (1980)
9. Bashford D., Chothia C. and Lesk A M.: Determinants of a protein fold. Unique features of the globin
amino acid sequences. J. mol. BioI. 196: 199-216
(1987)
10. Bellelli A et al.: Haem disorder in two myoglobins:
comparison of reorientation rate. Biochem. J. 246:
787-789 (1987)
11. 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. physioI. Chern. 365: 321-334
(1984)
12. BijIholt M. and van Bruggen E. E J.: A model for the
architecture of the hemocyanin from the arthropod
Squilla mantis (Crustacea, Stomatopoda). Eur. J.
Biochem. 155: 339-344 (1986)
13. Biswanger H.: Theorie und Methoden der Enzymkinetik. Verlag Chemie, Weinheim 1979
14. 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)
15. Bogusz D. et al.: Functioning haemoglobin genes in
non-nodulating plants. Nature 331: 178-180 (1988)
16. Boisset N. et al.: Three-dimensional reconstruction of
native Androctonus australis hemocyanin. J. mol.
BioI. 216: 743-760 (1990)
17. Borgese T. A, Harrington J. P. and Hoffman D.:
Anadara ovalis hemoglobins: distinct dissociation and
ligand binding characteristics. Compo Biochem. PhysioI. Pt. B. 86: 155-165 (1987)
18. Borgese T. A et al.: Haemoglobin properties and
polymerization in the marine teleost Lophius americanus (goosefish). Compo Biochem. PhysioI. Pt. B
91: 663-670 (1988)
19. Braunitzer G. and Hiebll.: Molecular aspects of high
altitude respiration in birds (In German). Naturwissenschaften 75: 280-287 (1988)
20. 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.
Compo Biochem. PhysioI. Pt. A 85: 785-790 (1986)
21. Brittain T.: The Root effect. Compo Biochem. Physiol. Pt. B 86: 473-481 (1987)
22. Brittain T.: Co-operative functioning of the dimeric
haemoglobin obtained from the radular muscle of the
amphineurian mollusc Amaurochiton glaucus. Compo
Biochem. Physiol. Pt. B 96: 96-295 (1990)
23. Brix 0.: The adaptive significance of the reversed
Bohr and Root shifts in blood from the marine gastropod, Buccinum undatum. J. expo Zool. 221: 27-36
(1982)
24. Brix O. et al.: The chloride shift may faciliatate oxygen loading and unloading to/from the hemoglobin
from the brown bear (Ursus arctos L.). Compo Biochern. Physiol. Pt. B 95: 865-868 (1990)
25. Brouwer M. and Serigstad B.: Allosteric control in
Limulus polyphemus hemocyanin: Function relevance of interactions between hexamers. Biochemistry 28: 8819-27 (1989)
26. Brunori M. et al.: Is there a Root effect in Xenopus
hemoglobin? FEBS Letters 221: 161-166 (1987)
27. Bunn H. E: Regulation of hemoglobin function in
mammals. Amer. Zool. 20: 199-211 (1980)
28. Bunn H. E and Forget B. G.: Hemoglobin. Molecular, genetic and clinical aspects. Saunders, Washington 1986
29. Burnett L. E., Scholnick D. A and Mangum C. P.:
Temperature sensitivity of molluscan and arthropod
hemocyanins. BioI. Bull. 174: 153-162 (1988)
30. Cardellini P and Sala M.: Developmental time of the
hemoglobin transition in the anuran Bombina orientalis. Compo Biochem. Physiol. Pt. B 75: 259-262
(1983)
31. 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)
32. Cheng, J. E, Krane D. E. and Hardison R. c.: Nucleotide sequence and expression of rabbit globin
genes zeta-I, zeta-2 and zeta-3. Pseudogenes generated by block duplications are transcriptionally competent. J. BioI. Chern. 263: 9981-93 (1988)
33. Cirotto C. and Arangi I.: Koelliker haemoglobins in
developing chick embryo. Compo Biochem. PhysioI.
Pt. B 92: 103-109 (1989)
34. Clegg J. B.: Gene conversions in the horse a-globin
gene complex. Mol. BioI. EvoI. 4: 492-503 (1987)