159. Mura U. et aI.: Purine salvage as metabolite and
energy saving mechanism in Camelus dromedarius:
The recovery of guanine. Compo Biochem. PhysioI.
Pt. B 87: 157-160 (1987)
160. Musti A. M. et al.: The complete structure of the rat
thyroglobulin gene. Proc. Nat. Acad. Sci. USA 83:
323-327 (1986)
161. Nagata Y. and Akino T.: D-amino acids in mouse tissues are not of microbial origin. Experientia 46:
466-468 (1990)
162. Nakane M. et al.: Molecular cloning and expression
of cDNAs coding for soluble guanylate cyclase from
rat lung. J. BioI. Chern. 265: 16841-45 (1990)
163. Nakatani Y. et aI.: Comparison of human brain and
liver glutamate dehydrogenase cDNAs. Biochem.
biophys. Res. Commun. 149: 405-410 (1987)
164. Negri A., Massey V. and Williams C. H. jr.: DAspartate oxidase from beef kidney. Purification and
properties. J. bioI. Chern. 262: 10026-34 (1987)
165. Nimmo I. A.: The glutathione S-transferase activity in
the pyloric caeca of the rainbow trout, Salmo gairdneri.
Comp. Biochem. Physiol. Pt. B 83: 831-835 (1986)
166. Noguchi T., Fujiwara S. and Hayashi S.: Evolution of
allantoinase and allantoicase involved in urate
degradation in liver peroxisomes. A rapid purification
of amphibian allantoinase and allantoicase complex,
and its comparison with fish allantoinase and allantoicase. J. bioI. Chern. 261: 4221-23 (1986)
167. Nomura K., Suzuki N. and Matsumoto S.: Pulcherosine, a novel tyrosine-derived, trivalent cross-linking
amino acid from the fertilization envelope of sea
urchin embryo. Biochemistry 29: 4525-34 (1990)
168. Ochiai M. and Ashida M.: Purification of a ~-1,3glucan recognition protein in the prophenoloxidase
activating system from hemolymph of the silkworm,
Bombyx mori. J. BioI. Chern. 263: 12056-62 (1988)
169. Oda T., Funai T. and Ichiyama A.: Generation from a
single gene of two mRNAs that endode the mitochondrial and peroxisomal serine:pyruvate aminotransferase of rat liver. J. BioI. Chern. 265: 7513-19
(1990)
170. Ogawa H. et aI.: Human liver serine dehydratase.
cDNA cloning and sequence homology with hydroxyamino acid dehydratases from other sources. J. BioI.
Chern. 264: 15818-23 (1989)
171. Ohmiya Y., Suzuki S. and Kondo Y.: Isolation and
characterization of hagfish thyroid iodoprotein by its
non-thyroglobulin nature, very high iodine and carbohydrate contents and low hormone/iodine ratio.
Eur. J. Biochem. 182: 11-18 (1989)
172. Ohmiya Y. et aI.: Location of dehydroalanine residues in the amino acid sequence of bovine thyroglobulin. Identification of "donor" tyrosine sites for hormonogenesis in thyroglobulin. J. BioI. Chern. 265:
9066-71 (1990)
173. O'Leary K. A. and Tracy J. w.: Purification of three
cytosolic glutathione S-transferases from adult Schistosoma mansoni. Arch. Biochem. Biophys. 264: 1-12
(1988)
174. Osanai M and Yonezawa Y.: The occurrence of free
methylated amino acids, especially N-trimethyllysine,
in the silkworm, Bombyx mori. Compo Biochem.
Physiol. Pt. B 82: 569-574 (1985)
175. Overbaugh J. M. et al.: Purification and preliminary
characterization of a monomeric glutathione Stransferase from Tetrahymena thermophila. Arch.
Biochem. Biophys. 261: 227-234 (1988)
References
459
176. Packard G. C. and Packard M. J.: Patterns of nitrogen excretion by embryonic softshell turtles (Trionyx
spiniferus) developing in cleidoic eggs. Science
1049-50 (1983)
177. Palumbo G. et aI.: The earliest site of iodination in
thyroglobulin is residue number 5. J. BioI. Chern.
265: 8887-92 (1990)
178. Parma J. et al.: Structural organization of the 5'
region of the thyroglobulin gene, evidence for intron
loss and "exonization" during evolution. J. mol. BioI.
196: 769-779 (1987)
179. Pattanakitsakul S. N., Ratanaphan A. and Ruenwongsa P.: Comparative studies on thymidylate synthetase from P. berghei and mouse reticulocytes.
Compo Biochem. Physiol. Pt. B 80: 583-587 (1985)
180. Pegg A. E.: Recent advances in the biochemistry of
polyamines in eukaryotes. Biochem. J. 234: 249-262
(1986)
181. Perryman M. B. et aI.: Isolation and sequence analysis of a full-length cDNA for human M creatine
kinase. Biochem. biophys. Res. Commun. 140:
981-989 (1986)
182. Peter M. G., Grun L. and Forster H.: CP-MAS-C13NMR spectra of sclerotized insect cuticle and of chitin. Angew. Chern. Int. ed. engl. 23: 638-639 (1984)
183. Phillips M. A., Coffino P. and Wang C. C.: Trypanosoma brucei ornithine decarboxylase: enzyme purification, characterization, and expression in Escherichia coli. J. BioI. Chern. 263: 17933-41 (1988)
184. Pickett C. P. and Lu A. Y. H.: Glutathione Stransferases: Gene structure, regulation and function.
Annual Rev. Biochem. 58: 743-764 (1989)
185. van Pilsum J. F., Stephens G. C. and Taylor D.: Distribution of creatine, guanidino-acetate and the enzymes for their biosynthesis in the animal kingdom.
Biochem. J. 126: 325-345 (1972)
186. Pol S. et al.: Nucleotide sequence and tissue distribution of the human mitochondrial aspartate aminotransferase mRNA. Biochem. biophys. Res. Commun. 157: 1309-15 (1988)
187. Poulin R., Larochelle J. and Nadeau P.: Polyamines
in Acanthamoeba castellanii: Presence of an unusually high, osmotically sensitive pool of 1,3diaminopropane. Biochem. biophys. Res. Comrnun.
122: 388-393 (1984)
188. Powell J. F. et al.: The primary structure of bovine
monoamine oxidase type A. Comparison with peptide sequences of bovine monoamine oxidase type B
and other flavoenzymes. Biochem. J. 259: 407-413
(1989)
189. Prents P.: Distribution of arginase and other ornithine
cycle enzymes in the gut of the earthworm Lumbricus
terrestris L. and some physiological and comparative
implications. Compo Biochem. PhysioI. Pt. B 93:
509-515 (1989)
190. Preston R. L.: Occurrence of D-amino acids in higher
organisms: A survey of the distribution of D-amino
acids in marine invertebrates. Compo Biochem. Physiol. 87B: 55-62 (1987)
191. Prezioso G., Indiveri C. and Bonvino V.: Kinetic
characterization of L-glutamate dehydrogenase isolated from Drosophila melanogaster larvae. Compo
Biochem. Physiol. 80B: 1-4 (1985)
192. Psarianos C. G., Marmaras V. J. and Vournakis J. N.:
Tyrosine-4-0-B-glucoside in the Mediterranean fruitfly Ceratitis capitata. Insect Biochem. 15: 129-135
(1985)
energy saving mechanism in Camelus dromedarius:
The recovery of guanine. Compo Biochem. PhysioI.
Pt. B 87: 157-160 (1987)
160. Musti A. M. et al.: The complete structure of the rat
thyroglobulin gene. Proc. Nat. Acad. Sci. USA 83:
323-327 (1986)
161. Nagata Y. and Akino T.: D-amino acids in mouse tissues are not of microbial origin. Experientia 46:
466-468 (1990)
162. Nakane M. et al.: Molecular cloning and expression
of cDNAs coding for soluble guanylate cyclase from
rat lung. J. BioI. Chern. 265: 16841-45 (1990)
163. Nakatani Y. et aI.: Comparison of human brain and
liver glutamate dehydrogenase cDNAs. Biochem.
biophys. Res. Commun. 149: 405-410 (1987)
164. Negri A., Massey V. and Williams C. H. jr.: DAspartate oxidase from beef kidney. Purification and
properties. J. bioI. Chern. 262: 10026-34 (1987)
165. Nimmo I. A.: The glutathione S-transferase activity in
the pyloric caeca of the rainbow trout, Salmo gairdneri.
Comp. Biochem. Physiol. Pt. B 83: 831-835 (1986)
166. Noguchi T., Fujiwara S. and Hayashi S.: Evolution of
allantoinase and allantoicase involved in urate
degradation in liver peroxisomes. A rapid purification
of amphibian allantoinase and allantoicase complex,
and its comparison with fish allantoinase and allantoicase. J. bioI. Chern. 261: 4221-23 (1986)
167. Nomura K., Suzuki N. and Matsumoto S.: Pulcherosine, a novel tyrosine-derived, trivalent cross-linking
amino acid from the fertilization envelope of sea
urchin embryo. Biochemistry 29: 4525-34 (1990)
168. Ochiai M. and Ashida M.: Purification of a ~-1,3glucan recognition protein in the prophenoloxidase
activating system from hemolymph of the silkworm,
Bombyx mori. J. BioI. Chern. 263: 12056-62 (1988)
169. Oda T., Funai T. and Ichiyama A.: Generation from a
single gene of two mRNAs that endode the mitochondrial and peroxisomal serine:pyruvate aminotransferase of rat liver. J. BioI. Chern. 265: 7513-19
(1990)
170. Ogawa H. et aI.: Human liver serine dehydratase.
cDNA cloning and sequence homology with hydroxyamino acid dehydratases from other sources. J. BioI.
Chern. 264: 15818-23 (1989)
171. Ohmiya Y., Suzuki S. and Kondo Y.: Isolation and
characterization of hagfish thyroid iodoprotein by its
non-thyroglobulin nature, very high iodine and carbohydrate contents and low hormone/iodine ratio.
Eur. J. Biochem. 182: 11-18 (1989)
172. Ohmiya Y. et aI.: Location of dehydroalanine residues in the amino acid sequence of bovine thyroglobulin. Identification of "donor" tyrosine sites for hormonogenesis in thyroglobulin. J. BioI. Chern. 265:
9066-71 (1990)
173. O'Leary K. A. and Tracy J. w.: Purification of three
cytosolic glutathione S-transferases from adult Schistosoma mansoni. Arch. Biochem. Biophys. 264: 1-12
(1988)
174. Osanai M and Yonezawa Y.: The occurrence of free
methylated amino acids, especially N-trimethyllysine,
in the silkworm, Bombyx mori. Compo Biochem.
Physiol. Pt. B 82: 569-574 (1985)
175. Overbaugh J. M. et al.: Purification and preliminary
characterization of a monomeric glutathione Stransferase from Tetrahymena thermophila. Arch.
Biochem. Biophys. 261: 227-234 (1988)
References
459
176. Packard G. C. and Packard M. J.: Patterns of nitrogen excretion by embryonic softshell turtles (Trionyx
spiniferus) developing in cleidoic eggs. Science
1049-50 (1983)
177. Palumbo G. et aI.: The earliest site of iodination in
thyroglobulin is residue number 5. J. BioI. Chern.
265: 8887-92 (1990)
178. Parma J. et al.: Structural organization of the 5'
region of the thyroglobulin gene, evidence for intron
loss and "exonization" during evolution. J. mol. BioI.
196: 769-779 (1987)
179. Pattanakitsakul S. N., Ratanaphan A. and Ruenwongsa P.: Comparative studies on thymidylate synthetase from P. berghei and mouse reticulocytes.
Compo Biochem. Physiol. Pt. B 80: 583-587 (1985)
180. Pegg A. E.: Recent advances in the biochemistry of
polyamines in eukaryotes. Biochem. J. 234: 249-262
(1986)
181. Perryman M. B. et aI.: Isolation and sequence analysis of a full-length cDNA for human M creatine
kinase. Biochem. biophys. Res. Commun. 140:
981-989 (1986)
182. Peter M. G., Grun L. and Forster H.: CP-MAS-C13NMR spectra of sclerotized insect cuticle and of chitin. Angew. Chern. Int. ed. engl. 23: 638-639 (1984)
183. Phillips M. A., Coffino P. and Wang C. C.: Trypanosoma brucei ornithine decarboxylase: enzyme purification, characterization, and expression in Escherichia coli. J. BioI. Chern. 263: 17933-41 (1988)
184. Pickett C. P. and Lu A. Y. H.: Glutathione Stransferases: Gene structure, regulation and function.
Annual Rev. Biochem. 58: 743-764 (1989)
185. van Pilsum J. F., Stephens G. C. and Taylor D.: Distribution of creatine, guanidino-acetate and the enzymes for their biosynthesis in the animal kingdom.
Biochem. J. 126: 325-345 (1972)
186. Pol S. et al.: Nucleotide sequence and tissue distribution of the human mitochondrial aspartate aminotransferase mRNA. Biochem. biophys. Res. Commun. 157: 1309-15 (1988)
187. Poulin R., Larochelle J. and Nadeau P.: Polyamines
in Acanthamoeba castellanii: Presence of an unusually high, osmotically sensitive pool of 1,3diaminopropane. Biochem. biophys. Res. Comrnun.
122: 388-393 (1984)
188. Powell J. F. et al.: The primary structure of bovine
monoamine oxidase type A. Comparison with peptide sequences of bovine monoamine oxidase type B
and other flavoenzymes. Biochem. J. 259: 407-413
(1989)
189. Prents P.: Distribution of arginase and other ornithine
cycle enzymes in the gut of the earthworm Lumbricus
terrestris L. and some physiological and comparative
implications. Compo Biochem. PhysioI. Pt. B 93:
509-515 (1989)
190. Preston R. L.: Occurrence of D-amino acids in higher
organisms: A survey of the distribution of D-amino
acids in marine invertebrates. Compo Biochem. Physiol. 87B: 55-62 (1987)
191. Prezioso G., Indiveri C. and Bonvino V.: Kinetic
characterization of L-glutamate dehydrogenase isolated from Drosophila melanogaster larvae. Compo
Biochem. Physiol. 80B: 1-4 (1985)
192. Psarianos C. G., Marmaras V. J. and Vournakis J. N.:
Tyrosine-4-0-B-glucoside in the Mediterranean fruitfly Ceratitis capitata. Insect Biochem. 15: 129-135
(1985)
