108. Linzen B. (ed.): Invertebrate oxygen carriers. Springer, Berlin 1986
109. Linzen B.: Blue blood. Structure and evolution of
hemocyanins (In German). Naturwissenschaften 76:
206-211 (1989).
110. 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)
111. Makino N.: Subunits of Panulirus japonicus hemocyanin. 2. Cooperativity of the homogonous hexamers.
Eur. J. Biochem. 173: 431-435 (1988)
112. Mangum C. P. (ed.): Blood and oxygen carriers.
Springer, New York 1992
113. Manwell C. and Baker C. M. A.: Magelona haemerythrin: tissues specificity, molecular weights and oxygen equilibiria. Compo Biochem. Physiol. Pt. B 89:
453-463 (1988)
114. Margot J. B., Demers G. Wand Hardison R. C.:
Complete nucleotide sequence of the rabbit ~-like
globin gene cluster. J. mol. BioI. 205: 15-40 (1989)
115. Markl J.: Evolution and function of structurally
diverse subunits in the respiratory protein hemocyanin from arthropods. BioI. Bull. 171: 90-115 (1986)
116. Mark! J. et al.: Quaternary and subunit structure of
Calliphora arylphorin as deduced from electron microscopy, electrophoresis, and sequence similarities
with arthropod hemocyanin. J. compo Physiol. B 162:
665-680 (1992)
117. 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)
118. Matsuura M. S. A., Fushitani K and Riggs A. F.: The
amino acid sequences of the a and ~ chains of hemoglobin from the snake, Liophis miliaris. J. BioI.
Chern. 264: 5515-21 (1989)
119. Mayr G. Wand 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)
120. Miller K. I. and Mangum C. P.: An investigation of
the nature of Bohr, Root, and Haldane effects in
Octopus dofleini hemocyanin. J. compo Physiol. B
158: 547-552 (1988)
121. 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)
122. 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)
123. 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)
124. Moon A. M. and Ley T. J.: Conservation of the primary structure, organization, and function of the
human and mouse ~-globin locus-activating regions.
Proc. Nat. Acad. Sci. USA 87: 7693-97 (1990)
125. Myers C. R. et al.: Haemoglobin-producing tissue of
larvae and pupae of Chironomus thummi (Diptera).
J. Insect Physiol. 32: 845-851 (1986)
126. Nakashima H. et al.: Structure of hemocyanin II from
the horseshoe crab, Limulus polyphemus. Sequences
of two overlapping peptides, ordering the CNBr fragReferences
285
ments, and the complete amino acid sequence. J.
bioI. Chern. 261: 10526-33 (1986)
127. Neuteboom B. et al.: Partial amino acid sequence of
a hemocyanin subunit from Palinurus vulgaris.
Compo Biochem. Physiol. Pt. B 94: 593-597 (1989)
128. Osmulski P. A. and Leyko W.: Structure, function and
physiological role of Chironomus haemoglobin
(Review). Compo Biochem. Physiol. Pt. B 85:
701-722 (1986)
129. Padgett R. W et al.: The molecular organization of
the beta-globin complex of the deer mouse, Peromyscus maniculatus. Mol. BioI. Evol. 4: 30-45 (1987)
130. Peeters K. et al.: The globin composition of Daphnia
pulex hemoglobin and the comparison of the amino
acid composition of invertebrate hemoglobins.
Compo Biochem. Physiol. Pt. B 97: 369-381 (1990)
131. Perutz M. F.: Species adaptation in a protein molecule. Mol. BioI. Evol. 1: 1-28 (1983)
132. Perutz M. F.: Species adaptation in a protein molecule. Adv. Protein Res. 36: 213-244 (1984)
133. Petruzzelli R. et al.: Amino acid sequence of a-chain
of hemoglobin IV from trout (Salmo irideus). Biochim. biophys. Acta 995: 255-258 (1989)
134. 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)
135. Powers D. A.: Molecular ecology of teleost fish
hemoglobins: strategies for adapting to changing
environments. Amer. Zool. 20: 139-162 (1980)
136. Reischl E. et al.: Bohr effect, electroin spin resonance spectroscopy and subunit dissociation of the
hemoglobin components from the turtle Phrynops
hilarii. Compo Biochem. PhysioI. Pt. B 78: 251-157
(1984)
137. Rendell M. et al.: An interspecies comparison of normal levels of glycosylated hemoglobin and glycosylated albumin. Compo Biochem. Physiol. Pt. B 81:
819-822 (1985)
138. Richardson D. E. et al.: Allosteric interactions in
sipunculid and brachiopod hemerythrins. Biochemistry 26: 1003-13 (1987)
139. Riggs A. F.: The Bohr effect. Annual Rev. Physiol.
50: 181-204 (1988)
140. Robinson I. B. and Ingram V. M.: Gene evolution in
the chicken ~-globin cluster. Cell 28: 515-521 (1982)
141. 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)
142. 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). BioI.
Chern. Hoppe-Seyler 370: 533-542 (1989)
143. Schartau W et al.: Hemocyanins in spiders. XIII.
Complete amino acid sequence of subunit a Eurypelma californicum. BioI. Chern. Hoppe-Seyler 371:
557-565 (1990)
144. Schimenti J. C. and Dumcan C. H.: Structure and
organization of the bovine ~-globin genes. Mol. BioI.
Evol. 2: 514-525 (1985)
145. Scott E. M. and Harrington J. P.: Methemoglobin
reductase activity in fish erythrocytes. Compo Biochern. PhysioI. Pt. B 82: 511-513 (1985)
109. Linzen B.: Blue blood. Structure and evolution of
hemocyanins (In German). Naturwissenschaften 76:
206-211 (1989).
110. 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)
111. Makino N.: Subunits of Panulirus japonicus hemocyanin. 2. Cooperativity of the homogonous hexamers.
Eur. J. Biochem. 173: 431-435 (1988)
112. Mangum C. P. (ed.): Blood and oxygen carriers.
Springer, New York 1992
113. Manwell C. and Baker C. M. A.: Magelona haemerythrin: tissues specificity, molecular weights and oxygen equilibiria. Compo Biochem. Physiol. Pt. B 89:
453-463 (1988)
114. Margot J. B., Demers G. Wand Hardison R. C.:
Complete nucleotide sequence of the rabbit ~-like
globin gene cluster. J. mol. BioI. 205: 15-40 (1989)
115. Markl J.: Evolution and function of structurally
diverse subunits in the respiratory protein hemocyanin from arthropods. BioI. Bull. 171: 90-115 (1986)
116. Mark! J. et al.: Quaternary and subunit structure of
Calliphora arylphorin as deduced from electron microscopy, electrophoresis, and sequence similarities
with arthropod hemocyanin. J. compo Physiol. B 162:
665-680 (1992)
117. 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)
118. Matsuura M. S. A., Fushitani K and Riggs A. F.: The
amino acid sequences of the a and ~ chains of hemoglobin from the snake, Liophis miliaris. J. BioI.
Chern. 264: 5515-21 (1989)
119. Mayr G. Wand 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)
120. Miller K. I. and Mangum C. P.: An investigation of
the nature of Bohr, Root, and Haldane effects in
Octopus dofleini hemocyanin. J. compo Physiol. B
158: 547-552 (1988)
121. 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)
122. 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)
123. 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)
124. Moon A. M. and Ley T. J.: Conservation of the primary structure, organization, and function of the
human and mouse ~-globin locus-activating regions.
Proc. Nat. Acad. Sci. USA 87: 7693-97 (1990)
125. Myers C. R. et al.: Haemoglobin-producing tissue of
larvae and pupae of Chironomus thummi (Diptera).
J. Insect Physiol. 32: 845-851 (1986)
126. Nakashima H. et al.: Structure of hemocyanin II from
the horseshoe crab, Limulus polyphemus. Sequences
of two overlapping peptides, ordering the CNBr fragReferences
285
ments, and the complete amino acid sequence. J.
bioI. Chern. 261: 10526-33 (1986)
127. Neuteboom B. et al.: Partial amino acid sequence of
a hemocyanin subunit from Palinurus vulgaris.
Compo Biochem. Physiol. Pt. B 94: 593-597 (1989)
128. Osmulski P. A. and Leyko W.: Structure, function and
physiological role of Chironomus haemoglobin
(Review). Compo Biochem. Physiol. Pt. B 85:
701-722 (1986)
129. Padgett R. W et al.: The molecular organization of
the beta-globin complex of the deer mouse, Peromyscus maniculatus. Mol. BioI. Evol. 4: 30-45 (1987)
130. Peeters K. et al.: The globin composition of Daphnia
pulex hemoglobin and the comparison of the amino
acid composition of invertebrate hemoglobins.
Compo Biochem. Physiol. Pt. B 97: 369-381 (1990)
131. Perutz M. F.: Species adaptation in a protein molecule. Mol. BioI. Evol. 1: 1-28 (1983)
132. Perutz M. F.: Species adaptation in a protein molecule. Adv. Protein Res. 36: 213-244 (1984)
133. Petruzzelli R. et al.: Amino acid sequence of a-chain
of hemoglobin IV from trout (Salmo irideus). Biochim. biophys. Acta 995: 255-258 (1989)
134. 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)
135. Powers D. A.: Molecular ecology of teleost fish
hemoglobins: strategies for adapting to changing
environments. Amer. Zool. 20: 139-162 (1980)
136. Reischl E. et al.: Bohr effect, electroin spin resonance spectroscopy and subunit dissociation of the
hemoglobin components from the turtle Phrynops
hilarii. Compo Biochem. PhysioI. Pt. B 78: 251-157
(1984)
137. Rendell M. et al.: An interspecies comparison of normal levels of glycosylated hemoglobin and glycosylated albumin. Compo Biochem. Physiol. Pt. B 81:
819-822 (1985)
138. Richardson D. E. et al.: Allosteric interactions in
sipunculid and brachiopod hemerythrins. Biochemistry 26: 1003-13 (1987)
139. Riggs A. F.: The Bohr effect. Annual Rev. Physiol.
50: 181-204 (1988)
140. Robinson I. B. and Ingram V. M.: Gene evolution in
the chicken ~-globin cluster. Cell 28: 515-521 (1982)
141. 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)
142. 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). BioI.
Chern. Hoppe-Seyler 370: 533-542 (1989)
143. Schartau W et al.: Hemocyanins in spiders. XIII.
Complete amino acid sequence of subunit a Eurypelma californicum. BioI. Chern. Hoppe-Seyler 371:
557-565 (1990)
144. Schimenti J. C. and Dumcan C. H.: Structure and
organization of the bovine ~-globin genes. Mol. BioI.
Evol. 2: 514-525 (1985)
145. Scott E. M. and Harrington J. P.: Methemoglobin
reductase activity in fish erythrocytes. Compo Biochern. PhysioI. Pt. B 82: 511-513 (1985)