124. Litthauer D., Naude R. J. and Oelofsen W.: Isolation, characterization and primary structure of two yLPH variants from ostrich pituitary glands. Int. J.
Peptide Protein Res. 24: 309-315 (1984)
125. Litthauer D. and Oelofsen W.: Purification and primary structure of ostrich pancreatic polypeptide. Int.
J. Peptide Protein Res. 29: 739-745 (1987)
126. Liu C. S. et al.: Pike eel (Muraenesox cinereus) gonadotropin. Amino acid sequences of both a and ~ subunits. Eur. J. Biochem. 186: 105-114 (1989)
127. de Loof A. and Schoofs L.: Homologies between the
amino acid sequences of some vertebrate peptide hormones and pep tides isolated from invertebrate sources (Minireview). Compo Biochem. Physiol. Pt. B 95:
459-468 (1990)
128. Lueschen W. et al.: Isolation, sequence analysis, and
physical properties of enkephalins in the neurons of
the shore crab, Carcinus maenas L. Proc. Nat. Acad.
Sci. USA 88: 8671-75 (1991)
129. Luo D. and McKeown B. A.: Immunological evidence of growth hormone-releasing factor-like substances in salmon (Oncorhynchus kisutch and O. keta).
Compo Biochem. Physiol. Pt. B 93: 615-620 (1989)
130. Maisonpierre P. C. et al.: Neurotrophin-3: A neurotrophic factor related to NGF and BDNR Science
247: 1446-51 (1990)
131. Majewski T. et al.: Isolation and amino acid sequence
of insullns and C-peptides of European bison (Bison
bonasus) and fox (Alopex lagopus). Int. J. Peptide
Protein Res. 30: 379-387 (1987)
132. Marshall J. et al.: Sequence and functional expression
of a single a-subunit of an insect nicotinic acetylcholine receptor. Embo J. 9: 4391-98 (1990)
133. Martens G. J. M.: Expression of two proopiomelanocortin genes in the pituitary gland of Xenopus laevis:
complete structures of the two prohormones. Nucleic
Acids Res. 14: 3791-98 (1986)
134. Marti T. et al.: Microanalysis of the amino acid
sequence of the eclosion hormone from the tobacco
homworm, Manduca sexta. FEBS Letters 219:
415-418 (1987)
135. Matsumoto S., Isogai A. and Suzuki A.: N-terminal
amino acid sequence of an insect neurohormone,
melanization and reddish coloration hormone
(MRCH): heterogeneity and sequence homology
with human insulin-like growth factor II. FEBS Letters 189: 115-118 (1985)
136. McDonald N. Q. and Blundell T. L.: Crystallization
and characterization of the high molecular weight
form of nerve growth factor (7S-NGF). J. mol. BioI.
219: 595-601 (1991)
137. Meakin S. O. and Shooter E. M.: lYrosine kinase
activity coupled to the high-affinity nerve growth factor receptor complex. Proc. Nat. Acad. Sci. USA 88:
5862-66 (1991)
138. Michel G. et al.: Evolutionary specificity of hydrins,
new hydroosmotic neuropeptides. Occurrence of
hydrin 2 (vasotocinyl-Gly) in the toad Bufo marinus
but not in the viper Vipera aspis. FEBS Letters 264:
135-137 (1990)
139. Miyawaki A. et al.: Structure-function relationships
of the mouse inositol-l,4,5-trisphosphate receptor.
Proc. Nat. Acad. Sci. USA 88: 4911-15 (1991)
140. Mizuno J. and Takeda N.: Phylogenetic study of the
arginine-vasotocinlarginine-vasopressin-like immunoreactive system in invertebrates. Compo Biochem.
Physiol. Pt. A 91: 739-747 (1988)
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141. Moffett R. B.: Purification of multiple forms of
plasma angiotensinogen: molecular weight and
charge heterogeneity. Biochim. biophys. Acta 912:
1-8 (1987)
142. Momota H. et al.: Amino acid sequence of flounder
growth hormone deduced from a cDNA sequence.
Nucleic Acids Res. 16: 10362 (1988)
143. Mor A., Delfour A. and Nicolas P.: Identification of a
D-alanine-containing polypeptide precursor for the
peptide opoid, dermorphin. J. BioI. Chem. 266:
6264-70 (1991)
144. Morel A. et al.: Prosomatostatin processing in anglerfish brain, gut, and pancreas. Biochem. biophys.
Res. Commun. 151: 347-354 (1988)
145. Morgan D. O. et al.: Insulin-like growth factor II
receptor as a multifunctional binding protein. Nature
329: 301-307 (1987)
146. Morley S. D. et al.: Vasotocin genes of the teleost fish
Catostomus commersoni: Gene structure, exonintron boundary, and hormone precursor organization. Biochemistry 29: 2506-11 (1990)
147. Muehlethaler M., Raggenbass M. and Dreifuss J. J.:
Peptides related to vasopressin in invertebrates.
Experientia 40: 777-782 (1984)
148. Nachman R. J. et al.: Leucosulfakinin, a sulfated
insect neuropeptide with homology to gastrin and
cholecystokinin. Science 234: 71-73 (1986)
149. Nachman R. J. et al.: Active conformation of an
insect neuropeptide family. Proc. Nat. Acad. Sci.
USA 88: 4518-22 (1991)
150. Nagamatsu S. et al.: Evolution of the insulin gene
superfamily: Sequence of a preproinsulin-like growth
factor cDNA from the Atlantic hagfish. J. BioI.
Chem. 266: 2397-2402 (1991)
151. Nagle G. T. et al.: Delta-bag cell peptide from the
egg-laying hormone precursor of Aplysia: Processing,
primary structure, and biological activity. J. BioI.
Chem. 265: 22329-35 (1990)
152. Nakagawa T. et al.: The subtypes of the mouse
inositol-l,4,5-trisphosphate receptor are expressed in
a tissue-specific and developmentally specific manner. Proc. Nat. Acad. Sci. USA 88: 6244-48 (1991)
153. Nakanishi S.: Substance P precursor and kininogen:
Their structures, gene organizations, and regulation.
Physiol. Rev. 67: 1117-42 (1987)
154. Nichols R., Schneuwly S. A. and Dixon, J. E.: Identification and characterization of a Drosophila homologue to the vertebrate neuropeptide cholecystokinin.
J. BioI. Chem. 263: 12167-70 (1988)
155. Noyes B. E. and Schaffer M. H.: The structurally
similar neuropeptides adipokinetic hormone I and II
are derived from similar, very small mRNAs. J. BioI.
Chem. 265: 483-489 (1990)
156. Nozaki M. et al.: Salmon pituitary gonadotropins. II.
Ontogeny of GTH I and GTH II cells in the rainbow
trout (Salmo gairdneri irideus). Gen. compo Endocrinol. 77: 358-367 (1990)
157. Oates K. K. and Erdos M.: Biochemical identification of thymosin alpha-I: its phylogenetic distribution
and evolutionary implications. Comp. Biochem. Physiol. Pt. B 94: 759-763 (1989)
158. Ohta N. et al.: Fulicin, a novel neuropeptide containing a D-amino acid residue isolated from the ganglia
of Achatina fulica. Biochem. biophys. Res. Commun.
178: 486-493 (1991)
159. Okawara Y. et al.: Cloning and sequence analysis of
cDNA for corticotropin-releasing factor precursor
Peptide Protein Res. 24: 309-315 (1984)
125. Litthauer D. and Oelofsen W.: Purification and primary structure of ostrich pancreatic polypeptide. Int.
J. Peptide Protein Res. 29: 739-745 (1987)
126. Liu C. S. et al.: Pike eel (Muraenesox cinereus) gonadotropin. Amino acid sequences of both a and ~ subunits. Eur. J. Biochem. 186: 105-114 (1989)
127. de Loof A. and Schoofs L.: Homologies between the
amino acid sequences of some vertebrate peptide hormones and pep tides isolated from invertebrate sources (Minireview). Compo Biochem. Physiol. Pt. B 95:
459-468 (1990)
128. Lueschen W. et al.: Isolation, sequence analysis, and
physical properties of enkephalins in the neurons of
the shore crab, Carcinus maenas L. Proc. Nat. Acad.
Sci. USA 88: 8671-75 (1991)
129. Luo D. and McKeown B. A.: Immunological evidence of growth hormone-releasing factor-like substances in salmon (Oncorhynchus kisutch and O. keta).
Compo Biochem. Physiol. Pt. B 93: 615-620 (1989)
130. Maisonpierre P. C. et al.: Neurotrophin-3: A neurotrophic factor related to NGF and BDNR Science
247: 1446-51 (1990)
131. Majewski T. et al.: Isolation and amino acid sequence
of insullns and C-peptides of European bison (Bison
bonasus) and fox (Alopex lagopus). Int. J. Peptide
Protein Res. 30: 379-387 (1987)
132. Marshall J. et al.: Sequence and functional expression
of a single a-subunit of an insect nicotinic acetylcholine receptor. Embo J. 9: 4391-98 (1990)
133. Martens G. J. M.: Expression of two proopiomelanocortin genes in the pituitary gland of Xenopus laevis:
complete structures of the two prohormones. Nucleic
Acids Res. 14: 3791-98 (1986)
134. Marti T. et al.: Microanalysis of the amino acid
sequence of the eclosion hormone from the tobacco
homworm, Manduca sexta. FEBS Letters 219:
415-418 (1987)
135. Matsumoto S., Isogai A. and Suzuki A.: N-terminal
amino acid sequence of an insect neurohormone,
melanization and reddish coloration hormone
(MRCH): heterogeneity and sequence homology
with human insulin-like growth factor II. FEBS Letters 189: 115-118 (1985)
136. McDonald N. Q. and Blundell T. L.: Crystallization
and characterization of the high molecular weight
form of nerve growth factor (7S-NGF). J. mol. BioI.
219: 595-601 (1991)
137. Meakin S. O. and Shooter E. M.: lYrosine kinase
activity coupled to the high-affinity nerve growth factor receptor complex. Proc. Nat. Acad. Sci. USA 88:
5862-66 (1991)
138. Michel G. et al.: Evolutionary specificity of hydrins,
new hydroosmotic neuropeptides. Occurrence of
hydrin 2 (vasotocinyl-Gly) in the toad Bufo marinus
but not in the viper Vipera aspis. FEBS Letters 264:
135-137 (1990)
139. Miyawaki A. et al.: Structure-function relationships
of the mouse inositol-l,4,5-trisphosphate receptor.
Proc. Nat. Acad. Sci. USA 88: 4911-15 (1991)
140. Mizuno J. and Takeda N.: Phylogenetic study of the
arginine-vasotocinlarginine-vasopressin-like immunoreactive system in invertebrates. Compo Biochem.
Physiol. Pt. A 91: 739-747 (1988)
References
315
141. Moffett R. B.: Purification of multiple forms of
plasma angiotensinogen: molecular weight and
charge heterogeneity. Biochim. biophys. Acta 912:
1-8 (1987)
142. Momota H. et al.: Amino acid sequence of flounder
growth hormone deduced from a cDNA sequence.
Nucleic Acids Res. 16: 10362 (1988)
143. Mor A., Delfour A. and Nicolas P.: Identification of a
D-alanine-containing polypeptide precursor for the
peptide opoid, dermorphin. J. BioI. Chem. 266:
6264-70 (1991)
144. Morel A. et al.: Prosomatostatin processing in anglerfish brain, gut, and pancreas. Biochem. biophys.
Res. Commun. 151: 347-354 (1988)
145. Morgan D. O. et al.: Insulin-like growth factor II
receptor as a multifunctional binding protein. Nature
329: 301-307 (1987)
146. Morley S. D. et al.: Vasotocin genes of the teleost fish
Catostomus commersoni: Gene structure, exonintron boundary, and hormone precursor organization. Biochemistry 29: 2506-11 (1990)
147. Muehlethaler M., Raggenbass M. and Dreifuss J. J.:
Peptides related to vasopressin in invertebrates.
Experientia 40: 777-782 (1984)
148. Nachman R. J. et al.: Leucosulfakinin, a sulfated
insect neuropeptide with homology to gastrin and
cholecystokinin. Science 234: 71-73 (1986)
149. Nachman R. J. et al.: Active conformation of an
insect neuropeptide family. Proc. Nat. Acad. Sci.
USA 88: 4518-22 (1991)
150. Nagamatsu S. et al.: Evolution of the insulin gene
superfamily: Sequence of a preproinsulin-like growth
factor cDNA from the Atlantic hagfish. J. BioI.
Chem. 266: 2397-2402 (1991)
151. Nagle G. T. et al.: Delta-bag cell peptide from the
egg-laying hormone precursor of Aplysia: Processing,
primary structure, and biological activity. J. BioI.
Chem. 265: 22329-35 (1990)
152. Nakagawa T. et al.: The subtypes of the mouse
inositol-l,4,5-trisphosphate receptor are expressed in
a tissue-specific and developmentally specific manner. Proc. Nat. Acad. Sci. USA 88: 6244-48 (1991)
153. Nakanishi S.: Substance P precursor and kininogen:
Their structures, gene organizations, and regulation.
Physiol. Rev. 67: 1117-42 (1987)
154. Nichols R., Schneuwly S. A. and Dixon, J. E.: Identification and characterization of a Drosophila homologue to the vertebrate neuropeptide cholecystokinin.
J. BioI. Chem. 263: 12167-70 (1988)
155. Noyes B. E. and Schaffer M. H.: The structurally
similar neuropeptides adipokinetic hormone I and II
are derived from similar, very small mRNAs. J. BioI.
Chem. 265: 483-489 (1990)
156. Nozaki M. et al.: Salmon pituitary gonadotropins. II.
Ontogeny of GTH I and GTH II cells in the rainbow
trout (Salmo gairdneri irideus). Gen. compo Endocrinol. 77: 358-367 (1990)
157. Oates K. K. and Erdos M.: Biochemical identification of thymosin alpha-I: its phylogenetic distribution
and evolutionary implications. Comp. Biochem. Physiol. Pt. B 94: 759-763 (1989)
158. Ohta N. et al.: Fulicin, a novel neuropeptide containing a D-amino acid residue isolated from the ganglia
of Achatina fulica. Biochem. biophys. Res. Commun.
178: 486-493 (1991)
159. Okawara Y. et al.: Cloning and sequence analysis of
cDNA for corticotropin-releasing factor precursor