104
3 The Structural Variety and Metabolism of Proteins
40. Combest W. L. and Gilbert L. I.: Particulate associated cAMP-dependent protein kinase activity in the
brain of the tobacco hornworm, Manduca sexta.
Insect Biochem. 19: 663-672 (1989)
41. Conlon J. M. and Thim L.: A peptide from the eel
pancreas with structural similarity to human pancreatic secretory trypsin inhibitor. Eur. J. Biochem.
174: 149-153 (1988)
42. Craik C. S., Rutter W. J. and Fletterick R.: Splice
junctions: association with variation in protein structure. Science 220: 1125-29 (1983)
43. Creighton T. E.: Protein folding. Biochem. J. 270:
1-16 (1990)
44. Dahlmann B. et aI.: The multicatalytic proteinase
(prosome) is ubiquitous from eukaryotes to archaebacteria. FEBS Letters 251: 125-131 (1989)
45. Dahms, N. M., Lobel P. and Kornfeld S.: Mannose 6phosphate receptors and lysosomal enzyme targeting
(Minireview). J. BioI. Chern. 264: 12115-18 (1989)
46. van Damme H. T. F. et aI.: Elongation factor I-beta
of Artemia: Localization of functional sites and
homology to elongation factor I-delta. Biochim. biophys. Acta 1050: 241-247 (1990)
47. Dang C. V. and Dang C. v.: Multienzyme complex of
aminoacyl-tRNA synthetases: an essence of being
eukaryotic (Review). Biochem. J. 239: 249-255
(1986)
48. Das S. et aI.: A cylic nucleotide-independent protein
kinase in Leishmania donovani. Biochem. J. 240:
641-649 (1986)
49. Davis, A. H., Nanduri J. and Watson D. C.: Cloning
and gene expression of Schistosoma mansoni protease. J. bioI. Chern. 262: 12851-55 (1987)
50. Davis C. A. et aI.: A gene family in Drosophila melanogaster coding for trypsin-like enzymes. Nucleic
Acids Res. 13: 6605-19 (1985)
51. Dayhof M. O. (ed.): Atlas of protein sequence and
structure, Vol. 5 and Suppi. 1-3. Nat. Biomed. Res.
Foundation, Washington 1972-78
52. Delbridge M. L. and Kelly L. E.: Sequence analysis
and chromosomal localization of a gene encoding a
cystatin-like protein from Drosophila melanogaster.
FEBS Letters 274: 141-145 (1990)
53. Dendinger J. E. and O'Connor K. L.: Purification
and characterization of a trypsin-like enzyme from
the midgut gland of the Atlantic blue crab, Callinectes sapidus. Compo Biochem. Physioi. Pt. B 95:
525-530 (1990)
54. Deng L. R. et aI.: Isolation and properties of two
allelic chymotrypsin inhibitors from the hemolymph
of the silkworm, Bombyx mori. Insect Biochem. 20:
531-536 (1990)
55. Diarra-Mehrpour M. et aI.: Human plasma inter-atrypsin inhibitor is encoded by four genes on three
chromosomes. Eur. J. Biochem. 179: 147-154 (1989)
56. Dje M. K. et aI.: Three genes under different developmental control encode elongation factor I-a in
Xenopus laevis. Nucleic Acids Res. 18: 3489-93
(1990)
57. Dombradi V. et aI.: Cloning and chromosomal localization of Drosophila cDNA encoding the catalytic
subunit of protein phosphatase la - High conservation between mammalian and insect sequences. Eur.
J. Biochem. 183: 603-610 (1989)
58. Donovan M. A. and Laue T. M.: A novel trypsin
inhibitor from the hemolymph of the horseshoe crab
Limulus polyphemus. J. BioI. Chern. 266: 2121-25
(1991)
59. Driscoll J. and Goldberg A. L.: The proteasome
(multicatalytic protease) is a component of the 1500kDa proteolytic complex which degrades ubiquitinconjugated proteins. J. BioI. Chern. 265: 4789-92
(1990)
60. Dufton M. J.: Proteinase inhibitors and dendrotoxins. Sequence classification, structural prediction and
structure/activity. Eur. J. Biochem. 153: 647-654
(1987)
61. Dunbar B. S.: Two-dimensional electrophoresis and
immunological techniques. Plenum, New York 1987
62. Dunwiddie C. et aI.: Antistasin, a leech-derived
inhibitor of factor Xa. Kinetic analysis of enzyme
inhibition and identification of the reactive site. J.
BioI. Chern. 264: 16695-99 (1989)
63. EdelmanA. M., Blumenthal D. K. and Krebs E. G.:
Protein serine/threonine kinases. Annual Rev. Biochern. 56: 567-613 (1987)
64. Ehlers M. R. W. et aI.: Molecular cloning of human
testicular angiotensin-converting enzyme: The testis
isozyme is identical to the C-terminal half of endothelial angiotensin-converting enzyme. Proc. Nat. Acad.
Sci. USA 86: 7741-45 (1989)
65. Enghild J. J. et al.: Alpha-macroglobulin from LimuIus polyphemus exhibits proteinase inhibitory activity
and participates in a hemolytic system. Biochemistry
29: 10070-80 (1990)
66. Estell D. A. and Laskowski M. jr.: Dermasterias
imbricata Trypsin I: an enzyme which rapidly hydrolyzes the reactive site peptide bonds of protein trypsin
inhibitors. Biochemistry 19: 124-131 (1980)
67. Falkenburg P. E. and Kloetzel P. M.: Identification
and characterization of three different subpopulations of the Drosophila multicatalytic proteinase
(proteasome). J. BioI. Chern. 264: 6660-66 (1989)
68. Fasman G. D. (ed.): Prediction of protein structure
and the principles of protein conformation. Plenum,
New York 1989
69. Faust P. L., Kornfeld S. and Chirgwin J. M.: Cloning
and sequence analysis of cDNA for human cathepsin
D. Proc. Nat. Acad. Sci. USA 82: 4910-14 (1985)
70. Feldman S. and Pizzo S. v.: Purification and characterization of frog a-macroglobulin: Receptor recognition of an amphibian glycoprotein. Biochemistry 24:
2569-75 (1985)
71. Fini M. E. et aI.: A gene for rabbit synovial cell collagenase: member of a family of metalloproteinases
that degrade the connective tissue matrix. Biochemistry 26: 6156-65 (1987)
72. Fischer E. H., Charbonneau H. and Tonks N. K.:
Protein tyrosine phosphatases. A diverse family of
intracellular and transmembrane enzymes. Science
253: 401-406 (1991)
73. Foleo E. J. et al.: Multicatalytic proteinase in fish
muscle. Arch. Biochem. Biophys. 267: 599-605
(1988)
74. Foster J. L., Higgins G. C. and Jackson F. R.: Cloning, sequence, and expression of the Drosophila
cAMP-dependent protein kinase catalytic subunit
gene. J. bioI. Chern. 263: 1676-81 (1988)
75. Freedman R. B. and Hawkins H. C. (eds.): The enzymology of posttranslational modification of proteins.
Acad. Press, New York 1985
76. Gabius H. J. et al.. Evolutionary aspects of accuracy
of phenylalananyl-tRNA synthetase. Accuracy of fun-
3 The Structural Variety and Metabolism of Proteins
40. Combest W. L. and Gilbert L. I.: Particulate associated cAMP-dependent protein kinase activity in the
brain of the tobacco hornworm, Manduca sexta.
Insect Biochem. 19: 663-672 (1989)
41. Conlon J. M. and Thim L.: A peptide from the eel
pancreas with structural similarity to human pancreatic secretory trypsin inhibitor. Eur. J. Biochem.
174: 149-153 (1988)
42. Craik C. S., Rutter W. J. and Fletterick R.: Splice
junctions: association with variation in protein structure. Science 220: 1125-29 (1983)
43. Creighton T. E.: Protein folding. Biochem. J. 270:
1-16 (1990)
44. Dahlmann B. et aI.: The multicatalytic proteinase
(prosome) is ubiquitous from eukaryotes to archaebacteria. FEBS Letters 251: 125-131 (1989)
45. Dahms, N. M., Lobel P. and Kornfeld S.: Mannose 6phosphate receptors and lysosomal enzyme targeting
(Minireview). J. BioI. Chern. 264: 12115-18 (1989)
46. van Damme H. T. F. et aI.: Elongation factor I-beta
of Artemia: Localization of functional sites and
homology to elongation factor I-delta. Biochim. biophys. Acta 1050: 241-247 (1990)
47. Dang C. V. and Dang C. v.: Multienzyme complex of
aminoacyl-tRNA synthetases: an essence of being
eukaryotic (Review). Biochem. J. 239: 249-255
(1986)
48. Das S. et aI.: A cylic nucleotide-independent protein
kinase in Leishmania donovani. Biochem. J. 240:
641-649 (1986)
49. Davis, A. H., Nanduri J. and Watson D. C.: Cloning
and gene expression of Schistosoma mansoni protease. J. bioI. Chern. 262: 12851-55 (1987)
50. Davis C. A. et aI.: A gene family in Drosophila melanogaster coding for trypsin-like enzymes. Nucleic
Acids Res. 13: 6605-19 (1985)
51. Dayhof M. O. (ed.): Atlas of protein sequence and
structure, Vol. 5 and Suppi. 1-3. Nat. Biomed. Res.
Foundation, Washington 1972-78
52. Delbridge M. L. and Kelly L. E.: Sequence analysis
and chromosomal localization of a gene encoding a
cystatin-like protein from Drosophila melanogaster.
FEBS Letters 274: 141-145 (1990)
53. Dendinger J. E. and O'Connor K. L.: Purification
and characterization of a trypsin-like enzyme from
the midgut gland of the Atlantic blue crab, Callinectes sapidus. Compo Biochem. Physioi. Pt. B 95:
525-530 (1990)
54. Deng L. R. et aI.: Isolation and properties of two
allelic chymotrypsin inhibitors from the hemolymph
of the silkworm, Bombyx mori. Insect Biochem. 20:
531-536 (1990)
55. Diarra-Mehrpour M. et aI.: Human plasma inter-atrypsin inhibitor is encoded by four genes on three
chromosomes. Eur. J. Biochem. 179: 147-154 (1989)
56. Dje M. K. et aI.: Three genes under different developmental control encode elongation factor I-a in
Xenopus laevis. Nucleic Acids Res. 18: 3489-93
(1990)
57. Dombradi V. et aI.: Cloning and chromosomal localization of Drosophila cDNA encoding the catalytic
subunit of protein phosphatase la - High conservation between mammalian and insect sequences. Eur.
J. Biochem. 183: 603-610 (1989)
58. Donovan M. A. and Laue T. M.: A novel trypsin
inhibitor from the hemolymph of the horseshoe crab
Limulus polyphemus. J. BioI. Chern. 266: 2121-25
(1991)
59. Driscoll J. and Goldberg A. L.: The proteasome
(multicatalytic protease) is a component of the 1500kDa proteolytic complex which degrades ubiquitinconjugated proteins. J. BioI. Chern. 265: 4789-92
(1990)
60. Dufton M. J.: Proteinase inhibitors and dendrotoxins. Sequence classification, structural prediction and
structure/activity. Eur. J. Biochem. 153: 647-654
(1987)
61. Dunbar B. S.: Two-dimensional electrophoresis and
immunological techniques. Plenum, New York 1987
62. Dunwiddie C. et aI.: Antistasin, a leech-derived
inhibitor of factor Xa. Kinetic analysis of enzyme
inhibition and identification of the reactive site. J.
BioI. Chern. 264: 16695-99 (1989)
63. EdelmanA. M., Blumenthal D. K. and Krebs E. G.:
Protein serine/threonine kinases. Annual Rev. Biochern. 56: 567-613 (1987)
64. Ehlers M. R. W. et aI.: Molecular cloning of human
testicular angiotensin-converting enzyme: The testis
isozyme is identical to the C-terminal half of endothelial angiotensin-converting enzyme. Proc. Nat. Acad.
Sci. USA 86: 7741-45 (1989)
65. Enghild J. J. et al.: Alpha-macroglobulin from LimuIus polyphemus exhibits proteinase inhibitory activity
and participates in a hemolytic system. Biochemistry
29: 10070-80 (1990)
66. Estell D. A. and Laskowski M. jr.: Dermasterias
imbricata Trypsin I: an enzyme which rapidly hydrolyzes the reactive site peptide bonds of protein trypsin
inhibitors. Biochemistry 19: 124-131 (1980)
67. Falkenburg P. E. and Kloetzel P. M.: Identification
and characterization of three different subpopulations of the Drosophila multicatalytic proteinase
(proteasome). J. BioI. Chern. 264: 6660-66 (1989)
68. Fasman G. D. (ed.): Prediction of protein structure
and the principles of protein conformation. Plenum,
New York 1989
69. Faust P. L., Kornfeld S. and Chirgwin J. M.: Cloning
and sequence analysis of cDNA for human cathepsin
D. Proc. Nat. Acad. Sci. USA 82: 4910-14 (1985)
70. Feldman S. and Pizzo S. v.: Purification and characterization of frog a-macroglobulin: Receptor recognition of an amphibian glycoprotein. Biochemistry 24:
2569-75 (1985)
71. Fini M. E. et aI.: A gene for rabbit synovial cell collagenase: member of a family of metalloproteinases
that degrade the connective tissue matrix. Biochemistry 26: 6156-65 (1987)
72. Fischer E. H., Charbonneau H. and Tonks N. K.:
Protein tyrosine phosphatases. A diverse family of
intracellular and transmembrane enzymes. Science
253: 401-406 (1991)
73. Foleo E. J. et al.: Multicatalytic proteinase in fish
muscle. Arch. Biochem. Biophys. 267: 599-605
(1988)
74. Foster J. L., Higgins G. C. and Jackson F. R.: Cloning, sequence, and expression of the Drosophila
cAMP-dependent protein kinase catalytic subunit
gene. J. bioI. Chern. 263: 1676-81 (1988)
75. Freedman R. B. and Hawkins H. C. (eds.): The enzymology of posttranslational modification of proteins.
Acad. Press, New York 1985
76. Gabius H. J. et al.. Evolutionary aspects of accuracy
of phenylalananyl-tRNA synthetase. Accuracy of fun-