gal and animal mitochondrial enzymes and their relationship to their cytoplasmic counterparts and a prokarytic enzyme. Biochemistry 22: 5306-15 (1983)
77. Gardell S. J. et al.: A novel rat carboxypeptidase,
CPA2: characterization, molecular cloning, and
evolutionary implications on substrate specificity in
the carboxypeptidase gene family. J. BioI. Chern.
263: 17828-36 (1988)
78. Gebhard W. et al.: Two out of the three kinds of subunits of inter-a-trypsin inhibitor are structurally
related. Eur. J. Biochem. 181: 571-576 (1989)
79. Ghersa P. et al.: Initiation of translation at a UAG
stop codon in the aldolase gene of Plasmodium falciparum. Embo J. 9: 1645-49 (1990)
80. Gildberg A.: Aspartic proteinases in fishes and
aquatic invertebrates. Compo Biochem. Physiol. Pt.
B 91: 425-35 (1988)
81. Gockel S. E and Lebherz H. G.: "Conformational"
isoenzymes in ascarid enolase. J. bioI. Chern. 256:
3877-83 (1981)
82. Godar D. E. et al.: Structural organization of the
multienzyme complex of mammalian aminoacyltRNA synthetases. Biochemistry 27: 6921-28 (1988)
83. Goldberg M. E.: The second translation of the genetic message: protein folding and assembly. Trends
biochem. Sci. 10: 388-391 (1985)
84. Gordon E. D. et al.: Eukaryotic initiation factor 4D,
the hypusine-containing protein, is conserved among
eukaryotes. J. bioI. Chern. 262: 16585-89 (1987)
85. Gordon J. I. et al.: Protein N-myristoylation (Minireview). J. BioI. Chern. 266: 8647-50 (1991)
86. Gould S. J. et al.: Peroxisomal protein import is conserved between yeast, plants, insects and mammals.
Embo J. 9: 85-90 (1990)
87. Grant G. A., Sacchettini J. C. and Welgus H. G.: A
collagenolytic serine protease with trypsin-like specificity from the fiddler crab Uca pugilator. Biochemistry 22: 354-358 (1983)
88. Grinblat Y., Brown N. H. and Kafatos E c.: Isolation
and characterization of the Drosophila translational
elongation factor 2 gene. Nucleic Acids Res. 17:
7303-14 (1989)
89. Gross R. E. et al.: Cloning, characterization, and
expression of the gene for the catalytic subunit of
cAMP-dependent protein kinase in Caenorhabditis
elegans. Identification of highly conserved and unique isoforms generated by alternative splicing. J.
BioI. Chern. 265: 6896-6907 (1990)
90. Grossman A.: Information transfer in biological systems. Targeting of proteins to specific organelles or to
the extracellular environment (secretion). Compo
Biochem. Physiol. Pt. B 91: 389-424 (1988)
91. Guerard E and Ie Gal Y.: Characterization of a
chymosin-like pepsin from the dogfish Scyliorhinus
canicula. Compo Biochem. Physiol. Pt. B 88: 823-827
(1987)
92. Gundersen R. E. and Nelson D. L.: A novel Cadependent protein kinase from Paramecium tetraurelia. J. bioI. Chern. 262: 4602-09 (1987)
93. Haass C. et al.: The Drosophila PROS-28.1 gene is a
member of the proteasome gene family. Gene 90:
235-241 (1990)
94. Hamed M. B. B. and Attias J.: Isolation and partial
characterization of two alkaline proteases of the
greater wax moth Galleria melonella (L.). Insect Biochern. 17: 653-658 (1987)
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95. Hameed, K. S. and Haard N. E: Isolation and characterization of cathepsin D from Atlantic short finned
squid Illex illecerebrosus. Compo Biochem. Physiol.
Pt. B 82: 241-246 (1985)
96. Hanks S. K., Quinn A. M. and Hunter T.: The protein kinase family: Conserved features and deduced
phylogeny of the catalytic domains. Science 241:
42-52 (1988)
97. Hansen L. J., Huang W. I. and J agus R.: Inhibitor of
translational initiation in sea urchin eggs prevents
mRNA utilization. J. bioI. Chern. 262: 6114-20 (1987)
98. Hardie D. G. and Coggins J. R. (eds.): Multidomain
proteins. Structure and funktion. Elsevier, Amsterdam 1986
99. Hartl E U. and Neupert W.: Protein sorting to mitochondria: Evolutionary conservations of folding and
assembly. Science 247: 930-938 (1990)
100. Hasty K. A. et al.: Human neutrophil collagenase. A
distinct gene product with homology to other matrix
metalloproteinases. J. BioI. Chern. 265: 11421-24
(1990)
101. Hayono T. et al.: Primary structure of human pepsinogen C gene. J. bioI. Chern. 263: 1382-85 (1988)
102. von Heijne G.: Signal sequences. The limits of variation. J. mol. BioI. 184: 99-105 (1985)
103. Helaakoski T. et al.: Molecular cloning of the asubunit of human prolyI4-hydroxylase: The complete
cDNA-derived amino acid sequence and evidence for
alternative splicing. Proc. Nat. Acad. Sci. USA 86:
4392-96 (1989)
104. van Hemert E J. et al.: The primary structure of
elongation factor EF-1a from the brine shrimp Artemia. Embo J. 3: 1109-13 (1984)
105. Hershey J. W. B.: Protein phosphorylation controls
translation rates. J. BioI. Chern. 264: 20823-26
(1989)
106. Hill R. E. and Hastie N. D.: Accelerated evolution in
the reactive center regions of serine protease inhibitors. Nature 326: 96-99 (1987)
107. Hille A. et al.: Occurrence of tyrosine sulfate in proteins. A balance sheet. 1. Secretory and lysosomal
proteins. Eur. J. Biochem. 188: 577-586 (1990)
108. Holm I. et al.: Evolution of aspartyl proteases by
gene duplication: the mouse renin gene is organized
in two homologous clusters of four exons. Embo J. 3:
557-562 (1984)
109. Holmes W. E. et al.: Primary structure of human a2antiplasmin, a serine protease inhibitor (serpin). J.
bioI. Chern. 262: 1659-64 (1987)
110. Holmquist R.: Evaluation of compositional nonrandomness in proteins. J. mol. Evol. 11: 349-360 (1978)
111. Horii A. et al.: On the cDNAs for two types of rat
pancreatic secretory trypsin inhibitor. Biochem. biophys. Res. Commun. 162: 151-159 (1989)
112. Houseman J. G. and Downe A. E. R.: Cathepsin Dlike activity in the posterior midgut of hemipteran
insects. Compo Biochem. Physiol. Pt. B 75: 509-512
(1983)
113. Houseman J. G., Campbell E C. and Morrison P. E.:
A preliminary characterization of digestive proteases
in the posterior midgut of the stable fly Stomoxys calcitrans (L.) (Diptera: Muscidae). Insect Biochem. 17:
213-218 (1987)
114. Hu E. and Rubin C. S.: Casein kinase II from Caenorhabditis elegans. Properties and developmental
regulation of the enzyme; cloning and sequence ana-
77. Gardell S. J. et al.: A novel rat carboxypeptidase,
CPA2: characterization, molecular cloning, and
evolutionary implications on substrate specificity in
the carboxypeptidase gene family. J. BioI. Chern.
263: 17828-36 (1988)
78. Gebhard W. et al.: Two out of the three kinds of subunits of inter-a-trypsin inhibitor are structurally
related. Eur. J. Biochem. 181: 571-576 (1989)
79. Ghersa P. et al.: Initiation of translation at a UAG
stop codon in the aldolase gene of Plasmodium falciparum. Embo J. 9: 1645-49 (1990)
80. Gildberg A.: Aspartic proteinases in fishes and
aquatic invertebrates. Compo Biochem. Physiol. Pt.
B 91: 425-35 (1988)
81. Gockel S. E and Lebherz H. G.: "Conformational"
isoenzymes in ascarid enolase. J. bioI. Chern. 256:
3877-83 (1981)
82. Godar D. E. et al.: Structural organization of the
multienzyme complex of mammalian aminoacyltRNA synthetases. Biochemistry 27: 6921-28 (1988)
83. Goldberg M. E.: The second translation of the genetic message: protein folding and assembly. Trends
biochem. Sci. 10: 388-391 (1985)
84. Gordon E. D. et al.: Eukaryotic initiation factor 4D,
the hypusine-containing protein, is conserved among
eukaryotes. J. bioI. Chern. 262: 16585-89 (1987)
85. Gordon J. I. et al.: Protein N-myristoylation (Minireview). J. BioI. Chern. 266: 8647-50 (1991)
86. Gould S. J. et al.: Peroxisomal protein import is conserved between yeast, plants, insects and mammals.
Embo J. 9: 85-90 (1990)
87. Grant G. A., Sacchettini J. C. and Welgus H. G.: A
collagenolytic serine protease with trypsin-like specificity from the fiddler crab Uca pugilator. Biochemistry 22: 354-358 (1983)
88. Grinblat Y., Brown N. H. and Kafatos E c.: Isolation
and characterization of the Drosophila translational
elongation factor 2 gene. Nucleic Acids Res. 17:
7303-14 (1989)
89. Gross R. E. et al.: Cloning, characterization, and
expression of the gene for the catalytic subunit of
cAMP-dependent protein kinase in Caenorhabditis
elegans. Identification of highly conserved and unique isoforms generated by alternative splicing. J.
BioI. Chern. 265: 6896-6907 (1990)
90. Grossman A.: Information transfer in biological systems. Targeting of proteins to specific organelles or to
the extracellular environment (secretion). Compo
Biochem. Physiol. Pt. B 91: 389-424 (1988)
91. Guerard E and Ie Gal Y.: Characterization of a
chymosin-like pepsin from the dogfish Scyliorhinus
canicula. Compo Biochem. Physiol. Pt. B 88: 823-827
(1987)
92. Gundersen R. E. and Nelson D. L.: A novel Cadependent protein kinase from Paramecium tetraurelia. J. bioI. Chern. 262: 4602-09 (1987)
93. Haass C. et al.: The Drosophila PROS-28.1 gene is a
member of the proteasome gene family. Gene 90:
235-241 (1990)
94. Hamed M. B. B. and Attias J.: Isolation and partial
characterization of two alkaline proteases of the
greater wax moth Galleria melonella (L.). Insect Biochern. 17: 653-658 (1987)
References
105
95. Hameed, K. S. and Haard N. E: Isolation and characterization of cathepsin D from Atlantic short finned
squid Illex illecerebrosus. Compo Biochem. Physiol.
Pt. B 82: 241-246 (1985)
96. Hanks S. K., Quinn A. M. and Hunter T.: The protein kinase family: Conserved features and deduced
phylogeny of the catalytic domains. Science 241:
42-52 (1988)
97. Hansen L. J., Huang W. I. and J agus R.: Inhibitor of
translational initiation in sea urchin eggs prevents
mRNA utilization. J. bioI. Chern. 262: 6114-20 (1987)
98. Hardie D. G. and Coggins J. R. (eds.): Multidomain
proteins. Structure and funktion. Elsevier, Amsterdam 1986
99. Hartl E U. and Neupert W.: Protein sorting to mitochondria: Evolutionary conservations of folding and
assembly. Science 247: 930-938 (1990)
100. Hasty K. A. et al.: Human neutrophil collagenase. A
distinct gene product with homology to other matrix
metalloproteinases. J. BioI. Chern. 265: 11421-24
(1990)
101. Hayono T. et al.: Primary structure of human pepsinogen C gene. J. bioI. Chern. 263: 1382-85 (1988)
102. von Heijne G.: Signal sequences. The limits of variation. J. mol. BioI. 184: 99-105 (1985)
103. Helaakoski T. et al.: Molecular cloning of the asubunit of human prolyI4-hydroxylase: The complete
cDNA-derived amino acid sequence and evidence for
alternative splicing. Proc. Nat. Acad. Sci. USA 86:
4392-96 (1989)
104. van Hemert E J. et al.: The primary structure of
elongation factor EF-1a from the brine shrimp Artemia. Embo J. 3: 1109-13 (1984)
105. Hershey J. W. B.: Protein phosphorylation controls
translation rates. J. BioI. Chern. 264: 20823-26
(1989)
106. Hill R. E. and Hastie N. D.: Accelerated evolution in
the reactive center regions of serine protease inhibitors. Nature 326: 96-99 (1987)
107. Hille A. et al.: Occurrence of tyrosine sulfate in proteins. A balance sheet. 1. Secretory and lysosomal
proteins. Eur. J. Biochem. 188: 577-586 (1990)
108. Holm I. et al.: Evolution of aspartyl proteases by
gene duplication: the mouse renin gene is organized
in two homologous clusters of four exons. Embo J. 3:
557-562 (1984)
109. Holmes W. E. et al.: Primary structure of human a2antiplasmin, a serine protease inhibitor (serpin). J.
bioI. Chern. 262: 1659-64 (1987)
110. Holmquist R.: Evaluation of compositional nonrandomness in proteins. J. mol. Evol. 11: 349-360 (1978)
111. Horii A. et al.: On the cDNAs for two types of rat
pancreatic secretory trypsin inhibitor. Biochem. biophys. Res. Commun. 162: 151-159 (1989)
112. Houseman J. G. and Downe A. E. R.: Cathepsin Dlike activity in the posterior midgut of hemipteran
insects. Compo Biochem. Physiol. Pt. B 75: 509-512
(1983)
113. Houseman J. G., Campbell E C. and Morrison P. E.:
A preliminary characterization of digestive proteases
in the posterior midgut of the stable fly Stomoxys calcitrans (L.) (Diptera: Muscidae). Insect Biochem. 17:
213-218 (1987)
114. Hu E. and Rubin C. S.: Casein kinase II from Caenorhabditis elegans. Properties and developmental
regulation of the enzyme; cloning and sequence ana-