References
1. Abe K. et al.: Molecular cloning of a cysteine proteinase inhibitor of rice (oryzacystatin). Homology with
animal cystatins and transient expression in the ripening process of rice seeds. J. bioI. Chern. 262:
16793-97 (1987)
2. Adam S. A. et al.: Identification of specific binding
proteins for a nuclear location sequence. Nature 337:
276-279 (1989)
3. Aitken A. : Identification of protein consensus
sequences. VHC Pubs. (Horwood), New York 1990
4. Alexander M. E. and Dresden M. H.: Collagenolytic
enzymes from the starfish, Pyenopodia helianthoides.
Compo Biochem. Physiol. Pt. B 67: 505-509 (1980)
5. Argos P. and Rao J. K. M.: Relationships between
exons and the predicted structure of membranebound proteins. Biochim. biophys. Acta 827:
283-297 (1985)
6. Armstrong P. B. et al.: Structure of a2-macroglobulin
from the arthropod Limus polyphemus. J. BioI.
Chern. 266: 2526-30 (1991)
7. Arribas. c., Sampedro J. and Izquierdo M.: The ubiquitin genes in Drosophila melanogaster: transcription and polymorphism. Biochim. biophys. Acta 868:
119-127 (1986)
8. Baba T. et al.:Activation and maturation mechanisms
of boar acrosin zymogen based on the deduced primary structure. J. BioI. Chern. 264: 11920-27 (1989)
9. Baici A. and Seemiiller u.: Kinetics of the inhibition
of human leucocyte elastase by eglin from the leech
Hirudo medicinalis. Biochem. J. 218: 829-833 (1984)
10. Bao J. J. et al.: Molecular evolution of serpins:
Homologous structure of the human alantichymotrypsin and aI-antitrypsin genes. Biochemistry 26: 7755-59 (1987). Correction: Biochemistry
27: 8508 (1988)
11. Barrett A. J. and McDonald J. K.: Mammalian proteases, Vol. I: Endopeptidases. Acad Press, New York
1980
12. Barrett A. J.: The cystatins: a new class of peptidase
inhibitors. frends biochem. Sci. 12: 193-196
13. Baudys M. and Kostka Y.: Covalent structure of
chicken pepsinogen. Eur. J. Biochem. 136: 89-99
(1983)
14. Bauw G. et al.: Protein-electroblotting and -microsequencing strategies in generating protein data bases
from two-dimensional gels. Proc. Nat. Acad. Sci.
USA 86: 7701-05 (1989)
15. Berger F. G. and Baumann H.: An evolutionary
switch in tissue-specific gene expression. Abundant
expression of aI-antitrypsin in the kidney of a wild
mouse species. J. bioI. Chern. 260: 1160-65 (1985)
16. Blankenship D. T. et al.: Amino acid sequence of ghilanten: anticoagulant-antimetastatic principle of the
South American leech, Haementeria ghilianii. Biochern. biophys. Res. Commun. 166: 1384-89 (1990)
17. Bode W. et al.: The 2.0 A X-ray structure of chicken
egg white cystatin and its possible mode of interaction
with cysteine proteinases. Embo J. 7: 2593-99 (1988)
18. Bond J. S. and Butler P. E.: Intracellular proteases.
Annual Rev. Biochem. 56: 333-364 (1987)
19. Bork P.: Recognition of functional regions in primary
structures using a set of property patterns. FEBS Letters 257: 191-195 (1989)
References
103
20. Borst P.: How proteins get into microbodies (peroxisomes, glyoxysomes, glycosomes). Biochim. biophys.
Acta 866: 179-203 (1986)
21. Bradshaw R. A.: Protein translocations and turnover
in eukaryotic cells. Trends biochem. Sci. 14: 276-279
(1989)
22. Brenner S.: The molecular evolution of genes and
proteins: a tale of two serines. Nature 334: 528-530
(1988)
23. Brown C. M. et al.: Sequence analysis suggests that
tetra-nucleotides signal the termination of protein
synthesis in eukaryotes. Nucleic Acids Res. 18:
6339-45 (1990)
24. Candelas G. et al.: Translational pauses during a spider fibroin synthesis. Biochem. biophys. Res. Commun. 116: 1033-38 (1983)
25. Carling D. and Hardie D. G.: The substrate and
sequence specificity of the AMP-activated protein
kinase. Phosphorylation of glycogen synthase and
phosphorylase kinase. Biochim. biophys. Acta 1012:
81-86 (1989)
26. Carrell R. and Travis J.: aI-Antitrypsin and the serpins: variation and countervariation. Trends biochern. Sci. 10: 20-24 (1985)
27. Cavener D. E. and Ray S. c.: Eukaryotic start and
stop translation sites. Nucleic Acids Res. 19: 3185-92
(1991)
28. Chang P. K. and Dignam J. D.: Pimary structure of
alanyl-transfer RNA synthetase and the regulation of
its messenger RNA levels in Bombyx mori. J. BioI.
Chern. 265: 20898-906 (1990)
29. Chao S. et al.: Molecular cloning and primary stucture of rat aI-antitrypsin. Biochemistry 29: 323-329
(1990)
30. Chappell L. C. and Dresden M. H.: Purification of
cysteine proteinases from adult Schistosoma mansoni. Arch. Biochem. Biophys. 256: 560-568 (1987)
31. Charbonneau H. et al.: Human placenta proteintyrosine-phosphatase: Amino acid sequence and relationship to a family of receptor-like proteins. Proc.
Nat. Acad. Sci. USA 86: 5252-56 (1989)
32. Cheeseman M. T. and Gooding R. H.: Proteolytic
enzymes from tsetse flies, Glossina morsitans and
Glossina palpalis (Diptera: Glossinidae). Insect Biochern. 15: 677-680 (1985)
33. Chothia C. and Finkelstein A. Y.: The classification
and origins of protein folding patterns. Annual Rev.
Biochem. 59: 1007-1039 (1990)
34. Clark Y. M. and Curthoys P.: Cause of subunit heterogeneity in purified rat renal phosphate-dependent
glutaminase. J. bioI. Chern. 254: 4939-41 (1979)
35. Cochrane B. J. and Richmond R. C.: Studies of
esterase-6 in Drosophila melanogaster. 1. Genetics of
a posttranslational modification. Biochem. Genetics
17: 167-183 (1979)
36. Cohen P.: The structure and regulation of protein
phosphatases. Annual Rev. Biochem. 58: 453-508
(1989)
37. Cohen P. T. W. et al.: Protein serine threonine phosphatases - An expanding family. FEBS Letters 268:
355-359 (1990)
38. Colella R. et al.: Chicken white cystatin. Molecular
cloning, nucleotide sequence, and tissue distribution.
J. BioI. Chern. 264: 17164-69 (1989)
39. Collier I. E. et al.: The structure of the human skin
fibroblast collagenase gene. J. BioI. Chern. 263:
10711-13 (1988)
1. Abe K. et al.: Molecular cloning of a cysteine proteinase inhibitor of rice (oryzacystatin). Homology with
animal cystatins and transient expression in the ripening process of rice seeds. J. bioI. Chern. 262:
16793-97 (1987)
2. Adam S. A. et al.: Identification of specific binding
proteins for a nuclear location sequence. Nature 337:
276-279 (1989)
3. Aitken A. : Identification of protein consensus
sequences. VHC Pubs. (Horwood), New York 1990
4. Alexander M. E. and Dresden M. H.: Collagenolytic
enzymes from the starfish, Pyenopodia helianthoides.
Compo Biochem. Physiol. Pt. B 67: 505-509 (1980)
5. Argos P. and Rao J. K. M.: Relationships between
exons and the predicted structure of membranebound proteins. Biochim. biophys. Acta 827:
283-297 (1985)
6. Armstrong P. B. et al.: Structure of a2-macroglobulin
from the arthropod Limus polyphemus. J. BioI.
Chern. 266: 2526-30 (1991)
7. Arribas. c., Sampedro J. and Izquierdo M.: The ubiquitin genes in Drosophila melanogaster: transcription and polymorphism. Biochim. biophys. Acta 868:
119-127 (1986)
8. Baba T. et al.:Activation and maturation mechanisms
of boar acrosin zymogen based on the deduced primary structure. J. BioI. Chern. 264: 11920-27 (1989)
9. Baici A. and Seemiiller u.: Kinetics of the inhibition
of human leucocyte elastase by eglin from the leech
Hirudo medicinalis. Biochem. J. 218: 829-833 (1984)
10. Bao J. J. et al.: Molecular evolution of serpins:
Homologous structure of the human alantichymotrypsin and aI-antitrypsin genes. Biochemistry 26: 7755-59 (1987). Correction: Biochemistry
27: 8508 (1988)
11. Barrett A. J. and McDonald J. K.: Mammalian proteases, Vol. I: Endopeptidases. Acad Press, New York
1980
12. Barrett A. J.: The cystatins: a new class of peptidase
inhibitors. frends biochem. Sci. 12: 193-196
13. Baudys M. and Kostka Y.: Covalent structure of
chicken pepsinogen. Eur. J. Biochem. 136: 89-99
(1983)
14. Bauw G. et al.: Protein-electroblotting and -microsequencing strategies in generating protein data bases
from two-dimensional gels. Proc. Nat. Acad. Sci.
USA 86: 7701-05 (1989)
15. Berger F. G. and Baumann H.: An evolutionary
switch in tissue-specific gene expression. Abundant
expression of aI-antitrypsin in the kidney of a wild
mouse species. J. bioI. Chern. 260: 1160-65 (1985)
16. Blankenship D. T. et al.: Amino acid sequence of ghilanten: anticoagulant-antimetastatic principle of the
South American leech, Haementeria ghilianii. Biochern. biophys. Res. Commun. 166: 1384-89 (1990)
17. Bode W. et al.: The 2.0 A X-ray structure of chicken
egg white cystatin and its possible mode of interaction
with cysteine proteinases. Embo J. 7: 2593-99 (1988)
18. Bond J. S. and Butler P. E.: Intracellular proteases.
Annual Rev. Biochem. 56: 333-364 (1987)
19. Bork P.: Recognition of functional regions in primary
structures using a set of property patterns. FEBS Letters 257: 191-195 (1989)
References
103
20. Borst P.: How proteins get into microbodies (peroxisomes, glyoxysomes, glycosomes). Biochim. biophys.
Acta 866: 179-203 (1986)
21. Bradshaw R. A.: Protein translocations and turnover
in eukaryotic cells. Trends biochem. Sci. 14: 276-279
(1989)
22. Brenner S.: The molecular evolution of genes and
proteins: a tale of two serines. Nature 334: 528-530
(1988)
23. Brown C. M. et al.: Sequence analysis suggests that
tetra-nucleotides signal the termination of protein
synthesis in eukaryotes. Nucleic Acids Res. 18:
6339-45 (1990)
24. Candelas G. et al.: Translational pauses during a spider fibroin synthesis. Biochem. biophys. Res. Commun. 116: 1033-38 (1983)
25. Carling D. and Hardie D. G.: The substrate and
sequence specificity of the AMP-activated protein
kinase. Phosphorylation of glycogen synthase and
phosphorylase kinase. Biochim. biophys. Acta 1012:
81-86 (1989)
26. Carrell R. and Travis J.: aI-Antitrypsin and the serpins: variation and countervariation. Trends biochern. Sci. 10: 20-24 (1985)
27. Cavener D. E. and Ray S. c.: Eukaryotic start and
stop translation sites. Nucleic Acids Res. 19: 3185-92
(1991)
28. Chang P. K. and Dignam J. D.: Pimary structure of
alanyl-transfer RNA synthetase and the regulation of
its messenger RNA levels in Bombyx mori. J. BioI.
Chern. 265: 20898-906 (1990)
29. Chao S. et al.: Molecular cloning and primary stucture of rat aI-antitrypsin. Biochemistry 29: 323-329
(1990)
30. Chappell L. C. and Dresden M. H.: Purification of
cysteine proteinases from adult Schistosoma mansoni. Arch. Biochem. Biophys. 256: 560-568 (1987)
31. Charbonneau H. et al.: Human placenta proteintyrosine-phosphatase: Amino acid sequence and relationship to a family of receptor-like proteins. Proc.
Nat. Acad. Sci. USA 86: 5252-56 (1989)
32. Cheeseman M. T. and Gooding R. H.: Proteolytic
enzymes from tsetse flies, Glossina morsitans and
Glossina palpalis (Diptera: Glossinidae). Insect Biochern. 15: 677-680 (1985)
33. Chothia C. and Finkelstein A. Y.: The classification
and origins of protein folding patterns. Annual Rev.
Biochem. 59: 1007-1039 (1990)
34. Clark Y. M. and Curthoys P.: Cause of subunit heterogeneity in purified rat renal phosphate-dependent
glutaminase. J. bioI. Chern. 254: 4939-41 (1979)
35. Cochrane B. J. and Richmond R. C.: Studies of
esterase-6 in Drosophila melanogaster. 1. Genetics of
a posttranslational modification. Biochem. Genetics
17: 167-183 (1979)
36. Cohen P.: The structure and regulation of protein
phosphatases. Annual Rev. Biochem. 58: 453-508
(1989)
37. Cohen P. T. W. et al.: Protein serine threonine phosphatases - An expanding family. FEBS Letters 268:
355-359 (1990)
38. Colella R. et al.: Chicken white cystatin. Molecular
cloning, nucleotide sequence, and tissue distribution.
J. BioI. Chern. 264: 17164-69 (1989)
39. Collier I. E. et al.: The structure of the human skin
fibroblast collagenase gene. J. BioI. Chern. 263:
10711-13 (1988)