106
3 The Structural Variety and Metabolism of Proteins
lyses of cDNA and the gene for the catalytic subunit.
J. BioI. Chern. 265: 5072-80 (1990)
115. Hunter T.: A thousand and one protein kinases. Cell
50: 823-829 (1987)
116. Isackson P. J., Ullrich A. and Bradshaw R. A.:
Mouse 7 S nerve growth factor: Complete sequence
of a cDNA coding for the a-subunit precursor and its
relationship to serine proteases. Biochemistry 23:
5997-6002 (1984)
117. Ishihara T. et al.: Primary structure and transcriptional regulation of rat pepsinogen C gene. J. BioI.
Chern. 264: 10193-99 (1989)
118. Ito A. et al.: The complete primary structure of calcineurin A, a calmodulin binding protein homologous
with protein phosphatases 1 and 2A. Biochem. biophys. Res. Commun. 163: 1492-97 (1989)
119. Jaenicke R.: Protein folding. Local structures,
domains, subunits and assemblies. Biochemistry 30:
3147-61 (1991)
120. James M. N. G., Delbaere L. T. J. and Brayer G. D.:
Amino acid sequence alignment of bacterial and
mammalian pancreatic serine proteases based on
topological equivalences. Can. J. Biochem. 56:
396-402 (1978)
121. James M. N. G., Sielecki A. R.: Molecular structure
of an aspartic proteinase zymogen, at 1.8 A resolution. Nature 319: 33-38 (1986)
122. Jany K. D. and Haug H.: Amino acid sequence ofthe
chymotryptic protease II from the larvae of the hornet, Vespa crabo. FEBS Letters 158: 98-102 (1983)
123. Jennings M. L.: Topography of membrane proteins.
Annual Rev. Biochem. 58: 999-1027 (1989)
124. Jentsch, S., Seufert W. and Hauser H. P.: Genetic
analysis of the ubiquitin system (Review). Biochim.
biophys. Acta 1089: 127-139 (1991)
125. Jeppson J. O. and Laurell C. B.: The amino acid substitutions of human aI-antitrypsin M3, X and Z.
FEBS Letters 231: 327-330 (1988)
126. Joemval1 H., Hooeg J.-O. and Gustavsson A.-M.:
Methods in protein sequence analysis. Birkhaeuser,
Basel 1991
127. Jonnalagadda S. et al.: Multiple (a-NH-ubiquitin)
protein endoproteases in cells. J. BioI. Chern. 264:
10637-42 (1989)
128. Jordao B. P. and Terra W. R.: Distribution, properties, and functions of midgut carboxypeptidases and
dipeptidases from Musca domestica larvae. Arch.
Insect Biochem. Physiol. 11: 231-244 (1989)
129. Kageyama T. and Takahashi K.: The complete amino
acid sequence of monkey pepsinogen A. J. bioI.
Chern. 261: 4395-4405 (1986)
130. Kageyama T. and Takahashi K.: The complete amino
acid sequence of monkey progastricsin. J. bioI.
Chern. 261: 4406-19 (1986)
131. Kalderon D. and Rubin G. M.: cGMP-dependent
protein kinase genes in Drosophila. J. BioI. Chern.
264: 10738-48 (1989)
132. Kang P. J. et al.: Requirement for hsp70 in the mitochondrial matrix for translocation and folding of precursor proteins. Nature 348: 137-143 (1990)
133. Kanost M. R.: Isolation and characterization of four
serine proteinase inhibitors (serpins) from hemolymph of Manduca sexta. Insect Biochem. 20:
141-147 (1990)
134. Kato I. and Tominaga N.: Trypsin-subtilisin inhibitor
from Red Sea turtle eggwhite consists of two tandem
domains - one Kunitz - one of a new family. Fed.
Proc. Abstract of 67th Annual Meeting Nr. 3168
(1983)
135. Kato I. et al.: Chicken ovomucoid: Determination of
its amino acid sequence, determination of the trypsin
reactive site, and preparation of all three of its
domains. Biochemistry 26: 193-201 (1987)
136. Katunuma N., Umezawa H. and Holzer H. (eds.):
Proteinase inhibitors. Medical and biological aspects.
Springer, Berlin 1983
137. Kavanagh E. J. and Tillinghast E. K.: The alkaline
proteases of Argiope - II. Fractionation of protease
activity and isolation of a silk fibroin digesting protease. Compo Biochem. Physiol. Pt. B 74: 365-372
(1983)
138. Kawamura M., Wadano A. and Miura K.: Purification and characterization of insect cathepsin D. Insect
Biochem. 17: 77-83 (1987)
139. Kenny A. J. and Ingram J.: Is there a tripeptidyl peptidase in the renal brushborder membrane? Biochem.
J. 255: 373-376 (1988)
140. Kikkawa u., Kishimoto A. and Nishizuka Y.: The
protein kinase C family: Heterogeneity and its
implications. Annual Rev. Biochem. 58: 31-44 (1989)
141. Kikuchi Y. and Tamiya N.: Chemical taxonomy of the
hinge-ligament proteins of bivalves according to their
amino acid compositions. Biochem. J. 242: 505-510
(1987)
142. Kim P. S. and Baldwin R. L.: Intermediates in the
folding reactions of small proteins. Annual Rev. Biochern. 59: 631-660 (1990)
143. Kirchhoff L. V. et al.: Ubiquitin genes in trypanosomatidae. J. BioI. Chern. 263: 12698-704 (1988)
144. Klier H. J., Vonfigura K. and Pohlmann R.: Isolation
and analysis of the human 46-kDa mannose 6phosphate receptor gene. Eur. J. Biochem. 197:
23-28 (1991)
145. Klimova o. A. et al.: The isolation and properties of
collagenolytic proteases from crab hepatopancreas.
Biochem. biophys. Res. Commun. 166: 1411-20
(1990)
146. Koster A. et al.: Molecular cloning of the mouse 46kDa mannose 6-phosphate receptor (MPR-46). BioI.
Chern. Hoppe-Seyler 372: 297-300 (1991)
147. Kreil G.: Transfer of proteins across membranes.
Annual Rev. Biochem. 50: 317-348 (1981)
148. Kruh G. D. et al.: The complete coding sequence of
arg defines thr. Abelson subfamily of cytoplasmic
tyrosine kinases. Proc. Nat. Acad. Sci. USA 87:
5802-06 (1990)
149. Lane C. D. et al.: The sequestration, processing and
retention of honey-bee promelittin made in amphibian oocytes. Eur. J. Biochem. 113: 273-281 (1981)
150. Laskowski M. et al.: Amino acid sequences of ovomucoid third domain from 25 additional species of
birds. J. Protein Chern. 9: 715-726 (1990)
151. Laycock M. V. et aI.: Purification and characterization of a digestive cysteine proteinase from the American lobster (Homarus americanus). Biochem. J. 263:
439-444 (1989)
152. Lazure C. et aI.: The complete amino acid sequence
of rat submaxillary gland tonin does contain the
aspartic acid at the active site: confirmation by protein sequence analyses. Biochem. Cell BioI. 65:
321-337 (1987)
153. Lecroisey A. et aI.: Complete amino acid sequence of
the collagenase from the insect Hypoderma lineatum.
J. bioI. Chern. 262: 7546-51 (1987)
3 The Structural Variety and Metabolism of Proteins
lyses of cDNA and the gene for the catalytic subunit.
J. BioI. Chern. 265: 5072-80 (1990)
115. Hunter T.: A thousand and one protein kinases. Cell
50: 823-829 (1987)
116. Isackson P. J., Ullrich A. and Bradshaw R. A.:
Mouse 7 S nerve growth factor: Complete sequence
of a cDNA coding for the a-subunit precursor and its
relationship to serine proteases. Biochemistry 23:
5997-6002 (1984)
117. Ishihara T. et al.: Primary structure and transcriptional regulation of rat pepsinogen C gene. J. BioI.
Chern. 264: 10193-99 (1989)
118. Ito A. et al.: The complete primary structure of calcineurin A, a calmodulin binding protein homologous
with protein phosphatases 1 and 2A. Biochem. biophys. Res. Commun. 163: 1492-97 (1989)
119. Jaenicke R.: Protein folding. Local structures,
domains, subunits and assemblies. Biochemistry 30:
3147-61 (1991)
120. James M. N. G., Delbaere L. T. J. and Brayer G. D.:
Amino acid sequence alignment of bacterial and
mammalian pancreatic serine proteases based on
topological equivalences. Can. J. Biochem. 56:
396-402 (1978)
121. James M. N. G., Sielecki A. R.: Molecular structure
of an aspartic proteinase zymogen, at 1.8 A resolution. Nature 319: 33-38 (1986)
122. Jany K. D. and Haug H.: Amino acid sequence ofthe
chymotryptic protease II from the larvae of the hornet, Vespa crabo. FEBS Letters 158: 98-102 (1983)
123. Jennings M. L.: Topography of membrane proteins.
Annual Rev. Biochem. 58: 999-1027 (1989)
124. Jentsch, S., Seufert W. and Hauser H. P.: Genetic
analysis of the ubiquitin system (Review). Biochim.
biophys. Acta 1089: 127-139 (1991)
125. Jeppson J. O. and Laurell C. B.: The amino acid substitutions of human aI-antitrypsin M3, X and Z.
FEBS Letters 231: 327-330 (1988)
126. Joemval1 H., Hooeg J.-O. and Gustavsson A.-M.:
Methods in protein sequence analysis. Birkhaeuser,
Basel 1991
127. Jonnalagadda S. et al.: Multiple (a-NH-ubiquitin)
protein endoproteases in cells. J. BioI. Chern. 264:
10637-42 (1989)
128. Jordao B. P. and Terra W. R.: Distribution, properties, and functions of midgut carboxypeptidases and
dipeptidases from Musca domestica larvae. Arch.
Insect Biochem. Physiol. 11: 231-244 (1989)
129. Kageyama T. and Takahashi K.: The complete amino
acid sequence of monkey pepsinogen A. J. bioI.
Chern. 261: 4395-4405 (1986)
130. Kageyama T. and Takahashi K.: The complete amino
acid sequence of monkey progastricsin. J. bioI.
Chern. 261: 4406-19 (1986)
131. Kalderon D. and Rubin G. M.: cGMP-dependent
protein kinase genes in Drosophila. J. BioI. Chern.
264: 10738-48 (1989)
132. Kang P. J. et al.: Requirement for hsp70 in the mitochondrial matrix for translocation and folding of precursor proteins. Nature 348: 137-143 (1990)
133. Kanost M. R.: Isolation and characterization of four
serine proteinase inhibitors (serpins) from hemolymph of Manduca sexta. Insect Biochem. 20:
141-147 (1990)
134. Kato I. and Tominaga N.: Trypsin-subtilisin inhibitor
from Red Sea turtle eggwhite consists of two tandem
domains - one Kunitz - one of a new family. Fed.
Proc. Abstract of 67th Annual Meeting Nr. 3168
(1983)
135. Kato I. et al.: Chicken ovomucoid: Determination of
its amino acid sequence, determination of the trypsin
reactive site, and preparation of all three of its
domains. Biochemistry 26: 193-201 (1987)
136. Katunuma N., Umezawa H. and Holzer H. (eds.):
Proteinase inhibitors. Medical and biological aspects.
Springer, Berlin 1983
137. Kavanagh E. J. and Tillinghast E. K.: The alkaline
proteases of Argiope - II. Fractionation of protease
activity and isolation of a silk fibroin digesting protease. Compo Biochem. Physiol. Pt. B 74: 365-372
(1983)
138. Kawamura M., Wadano A. and Miura K.: Purification and characterization of insect cathepsin D. Insect
Biochem. 17: 77-83 (1987)
139. Kenny A. J. and Ingram J.: Is there a tripeptidyl peptidase in the renal brushborder membrane? Biochem.
J. 255: 373-376 (1988)
140. Kikkawa u., Kishimoto A. and Nishizuka Y.: The
protein kinase C family: Heterogeneity and its
implications. Annual Rev. Biochem. 58: 31-44 (1989)
141. Kikuchi Y. and Tamiya N.: Chemical taxonomy of the
hinge-ligament proteins of bivalves according to their
amino acid compositions. Biochem. J. 242: 505-510
(1987)
142. Kim P. S. and Baldwin R. L.: Intermediates in the
folding reactions of small proteins. Annual Rev. Biochern. 59: 631-660 (1990)
143. Kirchhoff L. V. et al.: Ubiquitin genes in trypanosomatidae. J. BioI. Chern. 263: 12698-704 (1988)
144. Klier H. J., Vonfigura K. and Pohlmann R.: Isolation
and analysis of the human 46-kDa mannose 6phosphate receptor gene. Eur. J. Biochem. 197:
23-28 (1991)
145. Klimova o. A. et al.: The isolation and properties of
collagenolytic proteases from crab hepatopancreas.
Biochem. biophys. Res. Commun. 166: 1411-20
(1990)
146. Koster A. et al.: Molecular cloning of the mouse 46kDa mannose 6-phosphate receptor (MPR-46). BioI.
Chern. Hoppe-Seyler 372: 297-300 (1991)
147. Kreil G.: Transfer of proteins across membranes.
Annual Rev. Biochem. 50: 317-348 (1981)
148. Kruh G. D. et al.: The complete coding sequence of
arg defines thr. Abelson subfamily of cytoplasmic
tyrosine kinases. Proc. Nat. Acad. Sci. USA 87:
5802-06 (1990)
149. Lane C. D. et al.: The sequestration, processing and
retention of honey-bee promelittin made in amphibian oocytes. Eur. J. Biochem. 113: 273-281 (1981)
150. Laskowski M. et al.: Amino acid sequences of ovomucoid third domain from 25 additional species of
birds. J. Protein Chern. 9: 715-726 (1990)
151. Laycock M. V. et aI.: Purification and characterization of a digestive cysteine proteinase from the American lobster (Homarus americanus). Biochem. J. 263:
439-444 (1989)
152. Lazure C. et aI.: The complete amino acid sequence
of rat submaxillary gland tonin does contain the
aspartic acid at the active site: confirmation by protein sequence analyses. Biochem. Cell BioI. 65:
321-337 (1987)
153. Lecroisey A. et aI.: Complete amino acid sequence of
the collagenase from the insect Hypoderma lineatum.
J. bioI. Chern. 262: 7546-51 (1987)