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59. Crisp E. A., Messer M. and Vandeberg J. L.: Changes
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marsupial, Monodelphis domestica. Physiol. Zool. 62:
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60. Cross M. et al.: Mouse lysozyme M gene: Isolation,
characterization, and expression studies. Proc. Nat.
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61. Crowley H. M., Woodward D. R. and Rose R. W:
Changes in milk composition during lactation in the
potoroo, Potorus tridactylus (marsupialia: Potoroinae). Aust. J. bioI. Sci. 41: 289-296 (1988)
62. Dabrowski K.: Gulonolactone oxidase is missing in
teleost fish, the direct photometric assay. BioI. Chern.
Hoppe-Seyler 371: 207-214 (1990)
63. D'Amore M. A. et al.: Complete sequence and organization of the murine B-glucuronidase gene. Biochemistry 27: 7131-40 (1988)
64. Dautigny A. et al.: cDNA and amino acid sequences of
rainbow trout (Onkorhynchus mykiss) lysozymes and
their implications for the evolution of lysozyme and
lactalbumin. J. mol. Evol. 32: 187-198 (1991)
65. Dekan G., Gabel C. and Farquhar M. G.: Sulfate contributes to the negative charge of podocalyxin, the
major sialoglycoprotein of the glomerular filtration
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(1991)
66. Dietrich C. P. et al.: Characteristic distribution of
heparan sulfates and chondroitin sulfates in tissues and
organs of the Ampullaridae Pomacea sp. Compo Biochern. Physiol. Pt. B 76: 695-698 (1983)
67. Doege K. J. et al.: Complete primary structure of the
rat cartilage proteoglycan core protein deduced from
cDNA clones. J. bioI. Chern. 262: 17757-67 (1987),
Correction 263: 10040 (1988)
68. Doege K. J. et al.: Complete coding sequence and
deduced primary structure of the human cartilage large
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BioI. Chern. 266: 894-902 (1991)
69. D'Surney S. J. and DeKloet S. R.: Biochemical characterization of lysozymes present in egg white of
selected species of anatid birds. Compo Biochem. Physiol. Pt. B 82: 555-558 (1985)
70. Dughia J. and Hardingham T. E.: The primary structure of human cartilage link protein. Nucleic Acids
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71. Duman J. G. et al.: Freeze-tolerance adaptations,
including haemolymph protein and lipoprotein nucleators, in the larvae of the cranefly Tipula trivittata. J.
Insect Physiol. 31: 1-8 (1985)
72. Dunn D. R and Liberman M. H.: Chitin in sea anemone shells. Science 221: 157-159 (1983)
73. Dykhuizen D. E., Harrison K. M. and Richardson B.
J.: Evolutionary implications of ascorbic acid production in the Australian lungfish. Experientia 36:
945-946 (1980)
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2262-66 (1985)
75. Eklund H. et al.: Molecular aspects of functional differences between alcohol and sorbitol dehydrogenases. Biochemistry 24: 8005-12 (1985)
76. Eklund H. et al.: Comparison of three classes of
human liver alcohol dehydrogenase: Emphasis on different substrate binding pockets. Eur. J. Biochem. 193:
303-310 (1990)
77. Endo T. et al.: Structures of the sugar chains of a major
glycoprotein present in the egg jelly coat of a starfish,
Asterias amurensis. Arch. Biochem. Biophys. 252:
105-112 (1987)
78. England B. P., Heberlein U. and Tjian R.: Purified
Drosophila transcription factor, Adh distal factor-1
(Adf-1), binds to sites in several Drosophila promoters
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5086-94 (1990)
79. Fievre S. et al.: Primary structure of a trisialylated oligosaccharide from human milk. Biochem. biophys.
Res. Commun. 177: 720-725 (1991)
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sequence analysis of a cDNA encoding rat liver a-Lfucosidase. Biochem. J. 264: 695-701 (1989)
81. Florkin M. and Stotz E. H.: Comprehensive biochemistry, Vol. 6. Elsevier, Amsterdam 1965
82. Fong W P. and Keung W M.: Substrate specificity of
human class I alcohol dehydrogenase homo- and heterodimers containing the B2 (oriental) subunit. Biochemistry 26: 5726-32 (1987)
83. Friedman S.: Carbohydrate metabolism. In: Kerkut
G. A. and Gilbert L. I. (eds.): Comprehensive insect
physiology, biochemistry and pharmacology, Vol. 10,
pp. 43-76. Pergamon Press, Oxford 1985
84. FuerstT. R., Knipple D. C. and Macintyre R. J.: Purification and characterization of B-galactosidase-1 from
Drosophila melanogaster. Insect Biochem. 17: 1163-71
(1987)
85. Fukamizo T. and Kramer K. J.: Mechanism of chitin
hydrolysis by the binary chitinase system in insect
moulting fluid. Insect Biochem. 15: 141-145 (1985)
86. Funke B. and Spindler K. D.: Characterization of chitinase from the brine shrimp Artemia. Compo Biochern. Physiol. Pt. B 94: 691-695 (1989)
87. Galand G.: First purification and characterization of a
sucrase-isomaltase from goose kidney microvillous
membrane. Biochim. biophys. Acta 1033: 35-40
(1990)
88. Galjart N. J. et al.: Mouse "protective protein":
cDNA cloning, sequence comparison, and expression.
J. BioI. Chern. 265: 4678-84 (1990)
89. Gallagher J. T. and Walker A.: Molecular distinctions
between heparan sulphate and heparin. Analysis of
sulphation patterns indicates that heparan sulphate
and heparin are separate families of N-sulphated polysaccharides. Biochem. J. 230: 665-674 (1985)
90. Garcin R et al.: Acetaldehyde oxidation in Drosophila melanogaster and Drosophila simulans: evidence
for the presence of an NAD-dependent dehydrogenase. Compo Biochem. Physiol. Pt. B 75: 205-210
(1983)
91. Gavilanes J. G. et al.: Pigeon egg white lysozyme. Purification, structural and enzymic characterization. Int. J. Peptide Protein Res. 20: 238-245
(1982)
physiology of protozoa, 2. ed., Vol 2, pp. 381-408.
Acad. Press, New York 1979
57. Collins P. M. and Munasinghe R. (eds.): Carbohydrates. Chapman & Hall, London 1987
58. Crisp E. A., Czolij R. and Messer M.: Absence of Bgalactosidase (lactase) activity from intestinal brush
borders of suckling macropods: Implications for
mechanism of lactose absorption. Compo Biochem.
Physiol. Pt. B 88: 923-927 (1987)
59. Crisp E. A., Messer M. and Vandeberg J. L.: Changes
in milk carbohydrates during lactation in a didelphid
marsupial, Monodelphis domestica. Physiol. Zool. 62:
1117-25 (1989)
60. Cross M. et al.: Mouse lysozyme M gene: Isolation,
characterization, and expression studies. Proc. Nat.
Acad. Sci. USA 85: 6232-36 (1988)
61. Crowley H. M., Woodward D. R. and Rose R. W:
Changes in milk composition during lactation in the
potoroo, Potorus tridactylus (marsupialia: Potoroinae). Aust. J. bioI. Sci. 41: 289-296 (1988)
62. Dabrowski K.: Gulonolactone oxidase is missing in
teleost fish, the direct photometric assay. BioI. Chern.
Hoppe-Seyler 371: 207-214 (1990)
63. D'Amore M. A. et al.: Complete sequence and organization of the murine B-glucuronidase gene. Biochemistry 27: 7131-40 (1988)
64. Dautigny A. et al.: cDNA and amino acid sequences of
rainbow trout (Onkorhynchus mykiss) lysozymes and
their implications for the evolution of lysozyme and
lactalbumin. J. mol. Evol. 32: 187-198 (1991)
65. Dekan G., Gabel C. and Farquhar M. G.: Sulfate contributes to the negative charge of podocalyxin, the
major sialoglycoprotein of the glomerular filtration
slits. Proc. Nat. Acad. Sci. USA 88: 5398-5402
(1991)
66. Dietrich C. P. et al.: Characteristic distribution of
heparan sulfates and chondroitin sulfates in tissues and
organs of the Ampullaridae Pomacea sp. Compo Biochern. Physiol. Pt. B 76: 695-698 (1983)
67. Doege K. J. et al.: Complete primary structure of the
rat cartilage proteoglycan core protein deduced from
cDNA clones. J. bioI. Chern. 262: 17757-67 (1987),
Correction 263: 10040 (1988)
68. Doege K. J. et al.: Complete coding sequence and
deduced primary structure of the human cartilage large
aggregating proteoglycan aggrecan: Human-specific
repeats, and additional alternatively spliced forms. J.
BioI. Chern. 266: 894-902 (1991)
69. D'Surney S. J. and DeKloet S. R.: Biochemical characterization of lysozymes present in egg white of
selected species of anatid birds. Compo Biochem. Physiol. Pt. B 82: 555-558 (1985)
70. Dughia J. and Hardingham T. E.: The primary structure of human cartilage link protein. Nucleic Acids
Res. 18: 1292 (1990)
71. Duman J. G. et al.: Freeze-tolerance adaptations,
including haemolymph protein and lipoprotein nucleators, in the larvae of the cranefly Tipula trivittata. J.
Insect Physiol. 31: 1-8 (1985)
72. Dunn D. R and Liberman M. H.: Chitin in sea anemone shells. Science 221: 157-159 (1983)
73. Dykhuizen D. E., Harrison K. M. and Richardson B.
J.: Evolutionary implications of ascorbic acid production in the Australian lungfish. Experientia 36:
945-946 (1980)
References
507
74. Edenberg H. J. et al.: Cloning and sequencing of
cDNA encoding the complete mouse liver alcohol
dehydrogenase. Proc. Nat. Acad. Sci. USA 82:
2262-66 (1985)
75. Eklund H. et al.: Molecular aspects of functional differences between alcohol and sorbitol dehydrogenases. Biochemistry 24: 8005-12 (1985)
76. Eklund H. et al.: Comparison of three classes of
human liver alcohol dehydrogenase: Emphasis on different substrate binding pockets. Eur. J. Biochem. 193:
303-310 (1990)
77. Endo T. et al.: Structures of the sugar chains of a major
glycoprotein present in the egg jelly coat of a starfish,
Asterias amurensis. Arch. Biochem. Biophys. 252:
105-112 (1987)
78. England B. P., Heberlein U. and Tjian R.: Purified
Drosophila transcription factor, Adh distal factor-1
(Adf-1), binds to sites in several Drosophila promoters
and activates transcription. J. BioI. Chern. 265:
5086-94 (1990)
79. Fievre S. et al.: Primary structure of a trisialylated oligosaccharide from human milk. Biochem. biophys.
Res. Commun. 177: 720-725 (1991)
80. Fisher K. J. and Aronson N. N. jr.: Isolation and
sequence analysis of a cDNA encoding rat liver a-Lfucosidase. Biochem. J. 264: 695-701 (1989)
81. Florkin M. and Stotz E. H.: Comprehensive biochemistry, Vol. 6. Elsevier, Amsterdam 1965
82. Fong W P. and Keung W M.: Substrate specificity of
human class I alcohol dehydrogenase homo- and heterodimers containing the B2 (oriental) subunit. Biochemistry 26: 5726-32 (1987)
83. Friedman S.: Carbohydrate metabolism. In: Kerkut
G. A. and Gilbert L. I. (eds.): Comprehensive insect
physiology, biochemistry and pharmacology, Vol. 10,
pp. 43-76. Pergamon Press, Oxford 1985
84. FuerstT. R., Knipple D. C. and Macintyre R. J.: Purification and characterization of B-galactosidase-1 from
Drosophila melanogaster. Insect Biochem. 17: 1163-71
(1987)
85. Fukamizo T. and Kramer K. J.: Mechanism of chitin
hydrolysis by the binary chitinase system in insect
moulting fluid. Insect Biochem. 15: 141-145 (1985)
86. Funke B. and Spindler K. D.: Characterization of chitinase from the brine shrimp Artemia. Compo Biochern. Physiol. Pt. B 94: 691-695 (1989)
87. Galand G.: First purification and characterization of a
sucrase-isomaltase from goose kidney microvillous
membrane. Biochim. biophys. Acta 1033: 35-40
(1990)
88. Galjart N. J. et al.: Mouse "protective protein":
cDNA cloning, sequence comparison, and expression.
J. BioI. Chern. 265: 4678-84 (1990)
89. Gallagher J. T. and Walker A.: Molecular distinctions
between heparan sulphate and heparin. Analysis of
sulphation patterns indicates that heparan sulphate
and heparin are separate families of N-sulphated polysaccharides. Biochem. J. 230: 665-674 (1985)
90. Garcin R et al.: Acetaldehyde oxidation in Drosophila melanogaster and Drosophila simulans: evidence
for the presence of an NAD-dependent dehydrogenase. Compo Biochem. Physiol. Pt. B 75: 205-210
(1983)
91. Gavilanes J. G. et al.: Pigeon egg white lysozyme. Purification, structural and enzymic characterization. Int. J. Peptide Protein Res. 20: 238-245
(1982)