284
7 Respiratory Pigments
72. di Iorio E. E. et al.: Kinetics of oxygen and carbon
monoxide binding to liver fluke (Dicrocoelium dendriticum) hemoglobin. J. bioI. Chern. 260: 2160-64
(1985)
73. Iwaasa H., Takagi T. and Shikama K.: Protozoan
hemoglobin from Tetrahymena pyriformis. Isolation,
characterization, and amino acid sequence. J. BioI.
Chern. 265: 8603-09 (1990)
74. Jannasch H. w.: Deepsea life on the basis of chemical
synthesis (In German). Naturwissenschaften 72:
285-290 (1985)
75. Jensen E B. et aI.: A three-state MWC analysis of
oxygenation in tench (TInca tinca) hemoglobin. J.
compo Physioi. B 160: 407-411 (1990)
76. Jhiang S. M. and Riggs A E: The structure of the
gene encoding chain c of the hemoglobin of the earthworm, Lumbricus terrestris. J. BioI. Chern. 264:
19003-08 (1989)
77. Johnson B. A: Structure and function of the hemocyanin from a semiterrestrial crab, Ocypode quadrata.
J. compo Physioi. B 157: 501-509 (1987)
78. Jones G. et al.: Molecular cloning, regulation, and
complete sequence of a hemocyanin-related, juvenile
hormone-suppressible protein from insect hemolymph. J. BioI. Chern. 265: 8596-8602 (1990)
79. Kapp O. H. et al.: Quaternary structure of the giant
extracellular hemoglobin of the leech Macrobdella
decora. J. mol. BioI. 213: 141-158 (1990)
80. Karlson S. and Nienhuis A. w.: Developmental regulation of human globin genes. Annual Rev. Biochem.
54: 1071-1108 (1985)
81. Kleinschmidt T. and Sgouros J. G.: Hemoglobin
sequences. BioI. Chern. Hoppe-Seyler 368: 579-615
(1987)
82. 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. BioI. Chern. HoppeSeyler 370: 839-845 (1989)
83. Klippenstein G. L.: Structural aspects of hemerythrin
and myohemerythrin. Amer. Zooi. 20: 39-51 (1980)
84. Knochel W. et al.: Globin evolution in the genus
Xenopus: Comparative analysis of cDNAs coding for
adult globin polypeptides of Xenopus borealis and
Xenopus tropica1is. J. mol. Evoi. 23: 211-223 (1986)
85. Kobayashi M., Nezu T. and Tanaka Y.: Hypoxic
induction of hemoglobin synthesis in Daphnia
magna. Compo Biochem. Physioi. Pt. A 97: 513-517
(1990)
86. Kolatkar P. R. et al.: Novel subunit structure
observed for noncooperative hemoglobin from Urechis caupo. J. bioI. Chern. 263: 3462-65 (1988)
87. Komiyama M. H. et aI.: Was the loss of the D-helix in
a-globin a functional neutral mutationTNature 352:
349-351 (1991)
88. Koop B. E and Goodman M.: Evolutionary and
developmental aspects of two hemoglobin ~-chain
genes (epsilon-M and beta-M) of opossum. Proc.
Nat. Acad. Sci. USA 85: 3893-97 (1988)
89. Koop B. E et aI.: Tarsius delta- and beta-globin
genes: conversions, evolution and systematic implications. J. BioI. Chern. 264: 68-79 (1989)
90. Kortt A A, 'llinick M. J. and Appleby C. A.: Amino
acid sequences of hemoglobins I and II from root
nodules of the non-leguminous Parasponia rigidaRhizobium symbiosis, and a correction of the
sequence of hemoglobin I from Parasponia andersonii. Eur. J. Biochem. 175: 141-149 (1988)
91. van Kuik J. A. et aI.: Primary structure of the neutral
carbohydrate chains of hemocyanin from Panulirus
interruptus. Eur. J. Biochem. 159: 297-301 (1986)
92. van Kuik J. A. et al.: Primary structure of the acidic
carbohydrate chain of hemocyanin from Panulirus
interruptus. FEBS Letters 221: 150-154 (1987)
93. 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)
94. Lallier E and Truchot J. P.: Modulation of hemocyanin oxygen affinity by L-Iactate and urate in the
prawn Penaeus japonicus. J. expo BioI. 147: 133-146
(1989)
95. Landsmann J. et al.: Common evolutionary origin of
legume and non-legume plant haemoglobins. Nature
324: 166-168 (1986)
96. Lang W. H.: cDNA cloning of the Octopus dofleini
hemocyanin: Sequence of the carboxyl-terminal
domain. Biochemistry 27: 7276-82 (1988)
97. 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. BioI. 209: 235-247 (1989)
98. Lee A. W. and Karplus M.: Structure-specific model
of hemoglobin cooperativity. Proc. Nat. Acad. Sci.
USA 80: 7055-59 (1983)
99. 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. Biochern. 187: 617-625 (1990)
100. Lerch K. et al.: Different origins of metal binding
sites in binuclear copper proteins, tyrosinase and
hemocyanin. J. inorg. Biochem. 26: 213-217 (1986)
101. 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. BioI. 136: 225-270 (1980)
102. Leung S. 0., Proudfoot N. J. and Whitelaw E.: The
gene for theta-globin is transcribed in human fetal
erythroid tissues. Nature 329: 551-554 (1987)
103. Levy M. J. et al.: Isolation and characterization of
methemoglobin reductase from yellowfin tuna (Thunnus albacares). Compo Biochem. Physioi. Pt. B 81:
809-814 (1985)
104. Leyko W. and Osmulski P. A: Seasonal variability of
hemoglobin content and component composition of
Chironomus thummi larvae. Compo Biochem. Physioi. Pt. B 89: 613-616 (1985)
105. 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)
106. 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. bioI.
Chern. 261: 15327-33 (1986)
107. Lima A A. B. et al.: Allosteric effect of protons and
adenosine triphosphate on hemoglobins from aquatic
amphibia. J. compo Physioi. B 155: 353-355 (1985)
7 Respiratory Pigments
72. di Iorio E. E. et al.: Kinetics of oxygen and carbon
monoxide binding to liver fluke (Dicrocoelium dendriticum) hemoglobin. J. bioI. Chern. 260: 2160-64
(1985)
73. Iwaasa H., Takagi T. and Shikama K.: Protozoan
hemoglobin from Tetrahymena pyriformis. Isolation,
characterization, and amino acid sequence. J. BioI.
Chern. 265: 8603-09 (1990)
74. Jannasch H. w.: Deepsea life on the basis of chemical
synthesis (In German). Naturwissenschaften 72:
285-290 (1985)
75. Jensen E B. et aI.: A three-state MWC analysis of
oxygenation in tench (TInca tinca) hemoglobin. J.
compo Physioi. B 160: 407-411 (1990)
76. Jhiang S. M. and Riggs A E: The structure of the
gene encoding chain c of the hemoglobin of the earthworm, Lumbricus terrestris. J. BioI. Chern. 264:
19003-08 (1989)
77. Johnson B. A: Structure and function of the hemocyanin from a semiterrestrial crab, Ocypode quadrata.
J. compo Physioi. B 157: 501-509 (1987)
78. Jones G. et al.: Molecular cloning, regulation, and
complete sequence of a hemocyanin-related, juvenile
hormone-suppressible protein from insect hemolymph. J. BioI. Chern. 265: 8596-8602 (1990)
79. Kapp O. H. et al.: Quaternary structure of the giant
extracellular hemoglobin of the leech Macrobdella
decora. J. mol. BioI. 213: 141-158 (1990)
80. Karlson S. and Nienhuis A. w.: Developmental regulation of human globin genes. Annual Rev. Biochem.
54: 1071-1108 (1985)
81. Kleinschmidt T. and Sgouros J. G.: Hemoglobin
sequences. BioI. Chern. Hoppe-Seyler 368: 579-615
(1987)
82. 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. BioI. Chern. HoppeSeyler 370: 839-845 (1989)
83. Klippenstein G. L.: Structural aspects of hemerythrin
and myohemerythrin. Amer. Zooi. 20: 39-51 (1980)
84. Knochel W. et al.: Globin evolution in the genus
Xenopus: Comparative analysis of cDNAs coding for
adult globin polypeptides of Xenopus borealis and
Xenopus tropica1is. J. mol. Evoi. 23: 211-223 (1986)
85. Kobayashi M., Nezu T. and Tanaka Y.: Hypoxic
induction of hemoglobin synthesis in Daphnia
magna. Compo Biochem. Physioi. Pt. A 97: 513-517
(1990)
86. Kolatkar P. R. et al.: Novel subunit structure
observed for noncooperative hemoglobin from Urechis caupo. J. bioI. Chern. 263: 3462-65 (1988)
87. Komiyama M. H. et aI.: Was the loss of the D-helix in
a-globin a functional neutral mutationTNature 352:
349-351 (1991)
88. Koop B. E and Goodman M.: Evolutionary and
developmental aspects of two hemoglobin ~-chain
genes (epsilon-M and beta-M) of opossum. Proc.
Nat. Acad. Sci. USA 85: 3893-97 (1988)
89. Koop B. E et aI.: Tarsius delta- and beta-globin
genes: conversions, evolution and systematic implications. J. BioI. Chern. 264: 68-79 (1989)
90. Kortt A A, 'llinick M. J. and Appleby C. A.: Amino
acid sequences of hemoglobins I and II from root
nodules of the non-leguminous Parasponia rigidaRhizobium symbiosis, and a correction of the
sequence of hemoglobin I from Parasponia andersonii. Eur. J. Biochem. 175: 141-149 (1988)
91. van Kuik J. A. et aI.: Primary structure of the neutral
carbohydrate chains of hemocyanin from Panulirus
interruptus. Eur. J. Biochem. 159: 297-301 (1986)
92. van Kuik J. A. et al.: Primary structure of the acidic
carbohydrate chain of hemocyanin from Panulirus
interruptus. FEBS Letters 221: 150-154 (1987)
93. 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)
94. Lallier E and Truchot J. P.: Modulation of hemocyanin oxygen affinity by L-Iactate and urate in the
prawn Penaeus japonicus. J. expo BioI. 147: 133-146
(1989)
95. Landsmann J. et al.: Common evolutionary origin of
legume and non-legume plant haemoglobins. Nature
324: 166-168 (1986)
96. Lang W. H.: cDNA cloning of the Octopus dofleini
hemocyanin: Sequence of the carboxyl-terminal
domain. Biochemistry 27: 7276-82 (1988)
97. 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. BioI. 209: 235-247 (1989)
98. Lee A. W. and Karplus M.: Structure-specific model
of hemoglobin cooperativity. Proc. Nat. Acad. Sci.
USA 80: 7055-59 (1983)
99. 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. Biochern. 187: 617-625 (1990)
100. Lerch K. et al.: Different origins of metal binding
sites in binuclear copper proteins, tyrosinase and
hemocyanin. J. inorg. Biochem. 26: 213-217 (1986)
101. 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. BioI. 136: 225-270 (1980)
102. Leung S. 0., Proudfoot N. J. and Whitelaw E.: The
gene for theta-globin is transcribed in human fetal
erythroid tissues. Nature 329: 551-554 (1987)
103. Levy M. J. et al.: Isolation and characterization of
methemoglobin reductase from yellowfin tuna (Thunnus albacares). Compo Biochem. Physioi. Pt. B 81:
809-814 (1985)
104. Leyko W. and Osmulski P. A: Seasonal variability of
hemoglobin content and component composition of
Chironomus thummi larvae. Compo Biochem. Physioi. Pt. B 89: 613-616 (1985)
105. 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)
106. 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. bioI.
Chern. 261: 15327-33 (1986)
107. Lima A A. B. et al.: Allosteric effect of protons and
adenosine triphosphate on hemoglobins from aquatic
amphibia. J. compo Physioi. B 155: 353-355 (1985)