154. Lee H., Simon J. A. and Lis J. T.: Structure and
expression of ubiquitin genes of Drosophila melanogaster. Mol. cell. BioI. 8: 4727-35 (1988)
155. Lee L. W et al.: Relationships among the subunits of
the high molecular weight proteinase, macropain
(proteasome). Biochim. biophys. Acta 1037: 178-185
(1990)
156. Lehuerou I. et al.: Isolation and nucleotide sequence
of a cDNA clone for bovine pancreatic anionic trypsinogen. Structural identity with the trypsin family.
Eur. J. Biochem. 193: 767-773 (1990)
157. Lepage T. and Gache C.: Purification and characterization of the sea urchin embryo hatching enzyme. J.
BioI. Chem. 264: 4787-93 (1989)
158. Light A. and lanska H.: Enterokinase (enteropeptidase): comparative aspects. Trends biochem. Sci. 14:
110-112 (1989)
159. Lin Y. M.: Characterization and peptidase specificity
of lugworm (Arenicola cristata) protease C. Compo
Biochem. Physiol. Pt. B 95: 745-753 (1990)
160. Litchfield D. W et al.: Subunit structure of casein
kinase II from bovine testis. Demonstration that the
a and a' subunits are distinct polypeptides. J. BioI.
Chem. 265: 7638-44 (1990)
161. Lu X. et al.: Cloning, structure, and expression ofthe
gene for a novel regulatory subunit of cDNAdependent protein kinase in Caenorhabditis elegans.
J. BioI. Chem. 265: 3293-3303 (1990)
162. Luaces A. L. and Barrett A. J.: Affinity purification
and biochemical characterization of histolysin, the
major cysteine proteinase of Entamoeba histolytica.
Biochem. J. 250: 903-909 (1988)
163. Ma Z. M., Grubbs J. H. and Sly W S.: Cloning,
sequencing, and functional characterization of the
murine 46-kDa mannose 6-phosphate receptor. J.
BioI. Chem. 266: 10589-95 (1991)
164. Macdonald R. J., Stary S. J. and Swift G. H.: Two
similar but nonallelic pancreatic trypsinogens. Nucleotide sequence of the cloned cDNAs. J. bioI. Chem
257: 9724-32 (1982)
165. Mahlke K. et al.: Sorting pathways for mitochondrial
inner membrane proteins. Eur. J. Biochem. 192:
551-555 (1990)
166. Mallya S. K. et al.: Characterization of 58-kilodalton
human neutrophil collagenase. Comparison with
human fibroblast collagenase. Biochemistry 29:
10628-34 (1990)
167. Marecum J. A.: A trypsin inhibitor from the coelomic
fluid of the sea star Asterias forbesi. BioI. Bull. 172:
357-361 (1987)
168. van Marrewijk W. A. and Ravesetin H. J. L.: Amino
acid metabolism of Astacus leptodactylus Esch. - I.
Composition of the free and protein-bound amino
acids in different organs of the crayfish. Compo Biochem. Physiol. Pt. B 47: 531-542 (1974)
169. Martinage A. et al.: Primary structure of histone H2B
from gonads of the starfish Asterias rubens. Identification of an N-dimethylproline residue at the aminoterminal. Eur. J. Biochem. 147: 351-359 (1985)
170. Martzen M. R. et al.: Primary structure of the major
pepsin inhibitor from the intestinal parasitic nematode Ascaris suum. Biochemistry 29: 7366-72 (1990)
171. Marumo K. and Waite H.: Prolyl4-hydroxylase in the
foot of the marine mussel Mytilus edulis L.: Purification and characterization. J. expo Zool. 244: 365-374
(1987)
References
107
172. Mateu M. G., Vicente O. and Sierra J. M.: Protein
synthesis in Drosophila melanogaster embryos - Purification and characterization of polypeptide chaininitiation factor 2. Eur. J. Biochem. 162: 221-229
(1987)
173. Matthews J. A., Brown J. W S. and Hall T. C.: Phaseolin mRNA is translated to yield glycosylated polypeptides in Xenopus oocytes. Nature 294: 175-176
(1981)
174. Mayer R. J. and Doherty E: Intracellular protein
catabolism: state of the art. FEBS Letters 198:
181-193 (1986)
175. McCammon J. A. and Harvey S. C. (eds.): Dynamics
of proteins and nucleic acids. Cambridge Univ. Press,
Cambridge 1987
176. McDonald J. K. and Barrett A. J.: Mammalian proteases, Vol. 2: Exopeptidases. Acad. Press, London
1986
177. McIllhinney R. A. J.: The facts of life: The importance and function of protein acylation. Trends biochem. Sci. 15: 387-391 (1990)
178. Mehta H. B. et al.: Structural studies on the eukaryotic chain initiation factor 2 from rabbit reticulocytes and brine shrimp Artemia embryos. Phosphorylation by the hemecontrolled repressor and casein
kinase II. J. bioI. Chem. 261: 6705-11 (1986)
179. Meloun B., Chechova D. and Jonakova Y.: Homologies in the structures of bull seminal plasma acrosin
inhibitors and comparison with other homologous
proteinase inhibitors of the Kazal type. HoppeSeyler's Z. physiol. Chem. 364: 1665-70 (1983)
180. Miglietta L. A. P. and Nelson D. L.: A novel cGMPdependent protein kinase from Paramecium. J. BioI.
Chem. 263: 16096-105 (1988)
181. Moestrup S. K. and Gliemann J.: Purification of the
rat hepatic a2-macroglobulin receptor as an
approximately 440-kDa single chain protein. J. BioI.
Chem. 264: 15574-77 (1989)
182. Moss D. W: Isoenzymes. Chapman & Hall, London
1982
183. Muramatsu T. and Morita T.: Anionic trypsin-like
enzymes from the crab Eriocheir japonicus De Haan
active in more acidic media. Compo Biochem. Physiol. Pt. B 70: 527-533 (1981)
184. Murdock L. L. et al.: Cysteine digestive proteinases
in Coleoptera. Compo Biochem. Physiol. Pt. B 87:
783-787 (1987)
185. Mykles D. L.: Purification and characterization of a
multicatalytic proteinase from crustacean muscle:
Comparison of latent and heat-activated forms. Arch.
Biochem. Biophys. 274: 216-228 (1989)
186. Nanbu M., Kobayashi K. and Horiuchi S.: Purification and characterization of cathepsin D-like proteinase from the tadpole tail of bullfrog, Rana catesbeiana. Compo Biochem. Physiol. Pt. B 89: 569-575
(1988)
187. Nelson R. B. and Siman R.: Clipsin, a chymotrypsinlike protease in rat brain which is irreversibly inhibited by al-antichymotrypsin. J. BioI. Chem. 265:
3836-43 (1990)
188. Nene Y. et al.: A single exon codes for the enzyme
domain of a protozoan cysteine protease. J. BioI.
Chem. 265: 18047-50 (1990)
189. Neurath H.: Evolution of proteolytic enzymes. Science 224: 350-357 (1984)
expression of ubiquitin genes of Drosophila melanogaster. Mol. cell. BioI. 8: 4727-35 (1988)
155. Lee L. W et al.: Relationships among the subunits of
the high molecular weight proteinase, macropain
(proteasome). Biochim. biophys. Acta 1037: 178-185
(1990)
156. Lehuerou I. et al.: Isolation and nucleotide sequence
of a cDNA clone for bovine pancreatic anionic trypsinogen. Structural identity with the trypsin family.
Eur. J. Biochem. 193: 767-773 (1990)
157. Lepage T. and Gache C.: Purification and characterization of the sea urchin embryo hatching enzyme. J.
BioI. Chem. 264: 4787-93 (1989)
158. Light A. and lanska H.: Enterokinase (enteropeptidase): comparative aspects. Trends biochem. Sci. 14:
110-112 (1989)
159. Lin Y. M.: Characterization and peptidase specificity
of lugworm (Arenicola cristata) protease C. Compo
Biochem. Physiol. Pt. B 95: 745-753 (1990)
160. Litchfield D. W et al.: Subunit structure of casein
kinase II from bovine testis. Demonstration that the
a and a' subunits are distinct polypeptides. J. BioI.
Chem. 265: 7638-44 (1990)
161. Lu X. et al.: Cloning, structure, and expression ofthe
gene for a novel regulatory subunit of cDNAdependent protein kinase in Caenorhabditis elegans.
J. BioI. Chem. 265: 3293-3303 (1990)
162. Luaces A. L. and Barrett A. J.: Affinity purification
and biochemical characterization of histolysin, the
major cysteine proteinase of Entamoeba histolytica.
Biochem. J. 250: 903-909 (1988)
163. Ma Z. M., Grubbs J. H. and Sly W S.: Cloning,
sequencing, and functional characterization of the
murine 46-kDa mannose 6-phosphate receptor. J.
BioI. Chem. 266: 10589-95 (1991)
164. Macdonald R. J., Stary S. J. and Swift G. H.: Two
similar but nonallelic pancreatic trypsinogens. Nucleotide sequence of the cloned cDNAs. J. bioI. Chem
257: 9724-32 (1982)
165. Mahlke K. et al.: Sorting pathways for mitochondrial
inner membrane proteins. Eur. J. Biochem. 192:
551-555 (1990)
166. Mallya S. K. et al.: Characterization of 58-kilodalton
human neutrophil collagenase. Comparison with
human fibroblast collagenase. Biochemistry 29:
10628-34 (1990)
167. Marecum J. A.: A trypsin inhibitor from the coelomic
fluid of the sea star Asterias forbesi. BioI. Bull. 172:
357-361 (1987)
168. van Marrewijk W. A. and Ravesetin H. J. L.: Amino
acid metabolism of Astacus leptodactylus Esch. - I.
Composition of the free and protein-bound amino
acids in different organs of the crayfish. Compo Biochem. Physiol. Pt. B 47: 531-542 (1974)
169. Martinage A. et al.: Primary structure of histone H2B
from gonads of the starfish Asterias rubens. Identification of an N-dimethylproline residue at the aminoterminal. Eur. J. Biochem. 147: 351-359 (1985)
170. Martzen M. R. et al.: Primary structure of the major
pepsin inhibitor from the intestinal parasitic nematode Ascaris suum. Biochemistry 29: 7366-72 (1990)
171. Marumo K. and Waite H.: Prolyl4-hydroxylase in the
foot of the marine mussel Mytilus edulis L.: Purification and characterization. J. expo Zool. 244: 365-374
(1987)
References
107
172. Mateu M. G., Vicente O. and Sierra J. M.: Protein
synthesis in Drosophila melanogaster embryos - Purification and characterization of polypeptide chaininitiation factor 2. Eur. J. Biochem. 162: 221-229
(1987)
173. Matthews J. A., Brown J. W S. and Hall T. C.: Phaseolin mRNA is translated to yield glycosylated polypeptides in Xenopus oocytes. Nature 294: 175-176
(1981)
174. Mayer R. J. and Doherty E: Intracellular protein
catabolism: state of the art. FEBS Letters 198:
181-193 (1986)
175. McCammon J. A. and Harvey S. C. (eds.): Dynamics
of proteins and nucleic acids. Cambridge Univ. Press,
Cambridge 1987
176. McDonald J. K. and Barrett A. J.: Mammalian proteases, Vol. 2: Exopeptidases. Acad. Press, London
1986
177. McIllhinney R. A. J.: The facts of life: The importance and function of protein acylation. Trends biochem. Sci. 15: 387-391 (1990)
178. Mehta H. B. et al.: Structural studies on the eukaryotic chain initiation factor 2 from rabbit reticulocytes and brine shrimp Artemia embryos. Phosphorylation by the hemecontrolled repressor and casein
kinase II. J. bioI. Chem. 261: 6705-11 (1986)
179. Meloun B., Chechova D. and Jonakova Y.: Homologies in the structures of bull seminal plasma acrosin
inhibitors and comparison with other homologous
proteinase inhibitors of the Kazal type. HoppeSeyler's Z. physiol. Chem. 364: 1665-70 (1983)
180. Miglietta L. A. P. and Nelson D. L.: A novel cGMPdependent protein kinase from Paramecium. J. BioI.
Chem. 263: 16096-105 (1988)
181. Moestrup S. K. and Gliemann J.: Purification of the
rat hepatic a2-macroglobulin receptor as an
approximately 440-kDa single chain protein. J. BioI.
Chem. 264: 15574-77 (1989)
182. Moss D. W: Isoenzymes. Chapman & Hall, London
1982
183. Muramatsu T. and Morita T.: Anionic trypsin-like
enzymes from the crab Eriocheir japonicus De Haan
active in more acidic media. Compo Biochem. Physiol. Pt. B 70: 527-533 (1981)
184. Murdock L. L. et al.: Cysteine digestive proteinases
in Coleoptera. Compo Biochem. Physiol. Pt. B 87:
783-787 (1987)
185. Mykles D. L.: Purification and characterization of a
multicatalytic proteinase from crustacean muscle:
Comparison of latent and heat-activated forms. Arch.
Biochem. Biophys. 274: 216-228 (1989)
186. Nanbu M., Kobayashi K. and Horiuchi S.: Purification and characterization of cathepsin D-like proteinase from the tadpole tail of bullfrog, Rana catesbeiana. Compo Biochem. Physiol. Pt. B 89: 569-575
(1988)
187. Nelson R. B. and Siman R.: Clipsin, a chymotrypsinlike protease in rat brain which is irreversibly inhibited by al-antichymotrypsin. J. BioI. Chem. 265:
3836-43 (1990)
188. Nene Y. et al.: A single exon codes for the enzyme
domain of a protozoan cysteine protease. J. BioI.
Chem. 265: 18047-50 (1990)
189. Neurath H.: Evolution of proteolytic enzymes. Science 224: 350-357 (1984)