286
7 Respiratory Pigments
146. Shaw J. P., Marks J. and Shen C. K. J.: Evidence that
the recently discovered theta-l-globin gene is functional in higher primates. Nature 326: 717-720 (1987)
147. Shehee W. R. et al.: Nucleotide sequence of the
BALB/c mouse j3-globin complex. J. mol. BioI. 205:
41-62 (1989)
148. Shishikura E et al.: Amino acid sequence of the
monomer subunit of the extracellular hemoglobin of
Lumbricus terrestris. J. bioI. Chem. 262: 3123-31
(1987)
149. 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)
150. Sizaret P. Y. et al.: A refined quaternary structure of
Androctonus australis hemocyanin. Eur. J. Biochem.
127: 501-506 (1982)
151. 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)
152. Stalder J. et al.: Primary structure and evolutionary
relationship between the adult a-globin genes and
their 5'-flanking regions of Xenopus laevis and Xenopus tropicalis. J. mol. Evol. 28: 64-71 (1989)
153. Standley P. R. et al.: The calcium, copper and zinc
content of some annelid extracellular haemoglobins.
Biochem. J. 249: 915-916 (1988)
154. Stem M. S. et al.: Amino acid sequence of the monomer subunit of the giant extracellular hemoglobin of
the aquatic oligochaete, Thbifex tubifex. Eur. J. Biochem. 194: 67-73 (1990)
155. Stoecker W. et al.: The quatenary structure of four
crustacean two-hexameric hemocyanins: immunocorrelation, stoichiometry, reassembly and topology of
individual subunits. J. compo Physiol. B 158: 271-289
(1988)
156. Suzuki T.: Amino acid sequence of myoglobin from
the mollusc Dolabella auricularia. J. bioI. Chem. 261:
3692-99 (1986)
157. Suzuki T.: Amino acid sequence of a major globin
from the sea cucumber Paracaudina chilensis. Biochim. biophys. Acta 998: 292-296 (1989)
158. Suzuki T. et al.: Hemoglobins from the two closely
related clams Barbatia lima and Barbatia virescens.
Comparison of their subunit structures and Nterminal sequence of the unusual two-domain chain.
Zool. Sci. 6: 269-281 (1989)
159. 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)
160. Suzuki T., Takagi T. and Gotoh T.: Primary structure
of the two linker chains of the extracellular hemoglobin from the polychaete Tylorrhynchus heterochaetus. J. BioI. Chem. 265: 12168-77 (1990)
161. Suzuki T., Takagi T. and Ohta S.: Primary structure of
a constituent polypeptide chain (AlII) of the giant
hemoglobin from the deep-sea tube worm Lamellibrachia. A possible hydrogen sulfide-binding site.
Biochemistry 266: 221-225 (1990)
162. Tam L. T., Gray G. P. and Riggs A. E: The hemoglobins of the bullfrog Rana catesbeiana. The structure
of the j3-chain of component C and the role of the
a-chain in the formation of intermolecular disulfide
bonds. J. bioI. Chem. 261: 8290-94 (1986)
163. Terwilliger R. C. and Terwilliger N. B.: Molluscan
hemoglobins (Review). Comp. Biochem. Physiol. Pt.
B 81: 255-261 (1985)
164. Terwilliger N. B. et al.: Bivalve hemocyanins - a
comparison with other molluscan hemocyanins.
Comp. Biochem. Physiol. Pt. B 89: 189-195 (1988)
165. Toulmond A., J ouin C. and de Frescheville J.: Hemocyanin of the protobranch bivalve mollusc Nucula
hanleyi Winckworth. Compo Biochem. Physiol. Pt. B
88: 71-74 (1987)
166. Trewitt P. M., Boyer D. R. and Bergstrom G.: Characterization of maternal haemoglobins in the eggs
and embryos of Chironomus thummi. J. Insect Physiol. 32: 963-969 (1986)
167. 'frotman C. N. A. et al.: The polymeric hemoglobin
molecule of Artemia. Interpretation of translated
cDNA sequence of nine domains. J. BioI. Chem. 266:
13789-95 (1991)
168. Utecht R. E. and Kurtzjr. 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)
169. 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)
170. Vandergon T. L. and Colacino J. M.: Characterization of hemoglobin from Phoronis architecta (Phoronida). Comp. Biochem. Physiol. Pt. B 94: 31-39
(1989)
171. 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. Compo Biochem. Physiol. Pt. B 81: 743-747
(1985)
172. 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)
173. Vincent K. A. and WIlson A. C.: Evolution and transcription of Old World monkey globin genes. J. mol.
BioI. 207: 465-479 (1989)
174. Vinogradov S. N. and Kapp O. H. (eds.): Structure
and function of invertebrate oxygen carriers. Springer, New York 1991
175. Vinogradov S. N., SharmaP. K. andWalzD. A.: Iron
and heme content of the extracellular hemoglobins
and chlorocruorins of annelids (Review). Comp. Biochem. Physiol. Pt. B 98: 187-194 (1991)
176. Vmogradov S. N. et al.: A dodecamer of globin
chains is the principal functioning subunit of the
extracellular hemoglobin of Lumbricus terrestris. J.
BioI. Chem. 266: 13091-96 (1991)
177. Voit R. and Feldmaierfuchs G.: Arthropod hemocyanins: Molecular cloning and sequencing of cDNAs
encoding the tarantula hemocyanin subunit-A and
subunit-E. J. BioI. Chem. 265: 19447-52 (1990)
178. Volbeda A. and HoI W. G. J.: Crystal structure of
hexameric haemocyanin from Panulirus interruptus
refined at 3.2 A resolution. J. mol. BioI. 209:
249-279 (1989)
7 Respiratory Pigments
146. Shaw J. P., Marks J. and Shen C. K. J.: Evidence that
the recently discovered theta-l-globin gene is functional in higher primates. Nature 326: 717-720 (1987)
147. Shehee W. R. et al.: Nucleotide sequence of the
BALB/c mouse j3-globin complex. J. mol. BioI. 205:
41-62 (1989)
148. Shishikura E et al.: Amino acid sequence of the
monomer subunit of the extracellular hemoglobin of
Lumbricus terrestris. J. bioI. Chem. 262: 3123-31
(1987)
149. 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)
150. Sizaret P. Y. et al.: A refined quaternary structure of
Androctonus australis hemocyanin. Eur. J. Biochem.
127: 501-506 (1982)
151. 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)
152. Stalder J. et al.: Primary structure and evolutionary
relationship between the adult a-globin genes and
their 5'-flanking regions of Xenopus laevis and Xenopus tropicalis. J. mol. Evol. 28: 64-71 (1989)
153. Standley P. R. et al.: The calcium, copper and zinc
content of some annelid extracellular haemoglobins.
Biochem. J. 249: 915-916 (1988)
154. Stem M. S. et al.: Amino acid sequence of the monomer subunit of the giant extracellular hemoglobin of
the aquatic oligochaete, Thbifex tubifex. Eur. J. Biochem. 194: 67-73 (1990)
155. Stoecker W. et al.: The quatenary structure of four
crustacean two-hexameric hemocyanins: immunocorrelation, stoichiometry, reassembly and topology of
individual subunits. J. compo Physiol. B 158: 271-289
(1988)
156. Suzuki T.: Amino acid sequence of myoglobin from
the mollusc Dolabella auricularia. J. bioI. Chem. 261:
3692-99 (1986)
157. Suzuki T.: Amino acid sequence of a major globin
from the sea cucumber Paracaudina chilensis. Biochim. biophys. Acta 998: 292-296 (1989)
158. Suzuki T. et al.: Hemoglobins from the two closely
related clams Barbatia lima and Barbatia virescens.
Comparison of their subunit structures and Nterminal sequence of the unusual two-domain chain.
Zool. Sci. 6: 269-281 (1989)
159. 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)
160. Suzuki T., Takagi T. and Gotoh T.: Primary structure
of the two linker chains of the extracellular hemoglobin from the polychaete Tylorrhynchus heterochaetus. J. BioI. Chem. 265: 12168-77 (1990)
161. Suzuki T., Takagi T. and Ohta S.: Primary structure of
a constituent polypeptide chain (AlII) of the giant
hemoglobin from the deep-sea tube worm Lamellibrachia. A possible hydrogen sulfide-binding site.
Biochemistry 266: 221-225 (1990)
162. Tam L. T., Gray G. P. and Riggs A. E: The hemoglobins of the bullfrog Rana catesbeiana. The structure
of the j3-chain of component C and the role of the
a-chain in the formation of intermolecular disulfide
bonds. J. bioI. Chem. 261: 8290-94 (1986)
163. Terwilliger R. C. and Terwilliger N. B.: Molluscan
hemoglobins (Review). Comp. Biochem. Physiol. Pt.
B 81: 255-261 (1985)
164. Terwilliger N. B. et al.: Bivalve hemocyanins - a
comparison with other molluscan hemocyanins.
Comp. Biochem. Physiol. Pt. B 89: 189-195 (1988)
165. Toulmond A., J ouin C. and de Frescheville J.: Hemocyanin of the protobranch bivalve mollusc Nucula
hanleyi Winckworth. Compo Biochem. Physiol. Pt. B
88: 71-74 (1987)
166. Trewitt P. M., Boyer D. R. and Bergstrom G.: Characterization of maternal haemoglobins in the eggs
and embryos of Chironomus thummi. J. Insect Physiol. 32: 963-969 (1986)
167. 'frotman C. N. A. et al.: The polymeric hemoglobin
molecule of Artemia. Interpretation of translated
cDNA sequence of nine domains. J. BioI. Chem. 266:
13789-95 (1991)
168. Utecht R. E. and Kurtzjr. 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)
169. 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)
170. Vandergon T. L. and Colacino J. M.: Characterization of hemoglobin from Phoronis architecta (Phoronida). Comp. Biochem. Physiol. Pt. B 94: 31-39
(1989)
171. 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. Compo Biochem. Physiol. Pt. B 81: 743-747
(1985)
172. 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)
173. Vincent K. A. and WIlson A. C.: Evolution and transcription of Old World monkey globin genes. J. mol.
BioI. 207: 465-479 (1989)
174. Vinogradov S. N. and Kapp O. H. (eds.): Structure
and function of invertebrate oxygen carriers. Springer, New York 1991
175. Vinogradov S. N., SharmaP. K. andWalzD. A.: Iron
and heme content of the extracellular hemoglobins
and chlorocruorins of annelids (Review). Comp. Biochem. Physiol. Pt. B 98: 187-194 (1991)
176. Vmogradov S. N. et al.: A dodecamer of globin
chains is the principal functioning subunit of the
extracellular hemoglobin of Lumbricus terrestris. J.
BioI. Chem. 266: 13091-96 (1991)
177. Voit R. and Feldmaierfuchs G.: Arthropod hemocyanins: Molecular cloning and sequencing of cDNAs
encoding the tarantula hemocyanin subunit-A and
subunit-E. J. BioI. Chem. 265: 19447-52 (1990)
178. Volbeda A. and HoI W. G. J.: Crystal structure of
hexameric haemocyanin from Panulirus interruptus
refined at 3.2 A resolution. J. mol. BioI. 209:
249-279 (1989)