메뉴 건너뛰기




Volumn 142, Issue 3, 2005, Pages 308-316

Urea cycle of Fasciola gigantica: Purification and characterization of arginase

Author keywords

Amino acids; Arginase; Characterization; Fasciola gigantica; Purification; Urea cycle

Indexed keywords

AMINO ACID; ARGINASE; ARGININE; ARGININOSUCCINATE SYNTHASE; ARGINOSUCCINATE LYASE; CALCIUM ION; CANAVANINE; CARBAMATE KINASE; COBALT; ENZYME INHIBITOR; FERROUS ION; ISOLEUCINE; LEUCINE; LYSINE; MAGNESIUM ION; MERCURY; NICKEL; ORNITHINE; ORNITHINE CARBAMOYLTRANSFERASE; PROLINE; SEPHAROSE; UNCLASSIFIED DRUG; UREA; VALINE;

EID: 26844502929     PISSN: 10964959     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.cbpb.2005.08.002     Document Type: Article
Times cited : (24)

References (74)
  • 1
    • 0001428082 scopus 로고
    • Determination of citrulline and allantoin and demonstration of citrulline in blood plasma
    • R.M. Archibald Determination of citrulline and allantoin and demonstration of citrulline in blood plasma J. Biol. Chem. 156 1944 121 142
    • (1944) J. Biol. Chem. , vol.156 , pp. 121-142
    • Archibald, R.M.1
  • 2
    • 26844547069 scopus 로고
    • Sur l'activite arginasique du tissue hepatopancreatique d'Helix pomatia Lin. et d'Helix aspersa Mull
    • R. Baret, M. Mourgue, C. Girard, and J. et Charmot Sur l'activite arginasique du tissue hepatopancreatique d'Helix pomatia Lin. et d'Helix aspersa Mull C.R. Soc. Biol. 163 1969 459 466
    • (1969) C.R. Soc. Biol. , vol.163 , pp. 459-466
    • Baret, R.1    Mourgue, M.2    Girard, C.3    Et Charmot, J.4
  • 3
    • 17544399371 scopus 로고
    • Sur certaines properties des arginases du tissue hepatopancreatique d'Halix Pomatia Lin et d'Helix aspersa Mull.
    • R. Baret, C. Girard, and J. et Riou Sur certaines properties des arginases du tissue hepatopancreatique d'Halix Pomatia Lin Et d'Helix aspersa Mull. Biochimie 54 1972 421 430
    • (1972) Biochimie , vol.54 , pp. 421-430
    • Baret, R.1    Girard, C.2    Et Riou, J.3
  • 4
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding
    • M.M. Bradford A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding Anal. Biochem. 72 1976 248 254
    • (1976) Anal. Biochem. , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 5
    • 70449273818 scopus 로고
    • Comparative biochemistry of urea synthesis: I. Methods for the quantitative assay for urea cycle enzymes in liver
    • G.W. Brown, and P.P. Cohen Comparative biochemistry of urea synthesis: I. Methods for the quantitative assay for urea cycle enzymes in liver J. Biol. Chem. 234 1959 1769 1774
    • (1959) J. Biol. Chem. , vol.234 , pp. 1769-1774
    • Brown, G.W.1    Cohen, P.P.2
  • 6
    • 0002537754 scopus 로고
    • Comparative biochemistry of urea synthesis. 3. Activities of urea-cycle enzymes in various higher and lower vertebrates
    • G.W. Brown, and P.P. Cohen Comparative biochemistry of urea synthesis. 3. Activities of urea-cycle enzymes in various higher and lower vertebrates Biochem. J. 75 1960 82 91
    • (1960) Biochem. J. , vol.75 , pp. 82-91
    • Brown, G.W.1    Cohen, P.P.2
  • 7
    • 13144255097 scopus 로고
    • Studies on arginase and ureogenesis in the elasmobranch Mustelus canis
    • J.W. Campbell Studies on arginase and ureogenesis in the elasmobranch Mustelus canis Arch. Biochem. Biophys. 93 1961 448 455
    • (1961) Arch. Biochem. Biophys. , vol.93 , pp. 448-455
    • Campbell, J.W.1
  • 8
    • 0013905560 scopus 로고
    • A comparative study of molluscan and mammalian arginases
    • J.W. Campbell A comparative study of molluscan and mammalian arginases Comp. Biochem. Physiol. 18 1966 179 199
    • (1966) Comp. Biochem. Physiol. , vol.18 , pp. 179-199
    • Campbell, J.W.1
  • 9
    • 0022544933 scopus 로고
    • Kinetics of inhibition of rat liver and kidney arginases by proline and branched-chain amino acids
    • N. Carvajal, and S.D. Cederbaum Kinetics of inhibition of rat liver and kidney arginases by proline and branched-chain amino acids Biochim. Biophys. Acta 870 1986 181 184
    • (1986) Biochim. Biophys. Acta , vol.870 , pp. 181-184
    • Carvajal, N.1    Cederbaum, S.D.2
  • 11
    • 0023508037 scopus 로고
    • Subcellular localization and kinetic properties of arginase from the liver of Genypterus maculatus
    • N. Carvajal, E. Kessi, and L. Ainol Subcellular localization and kinetic properties of arginase from the liver of Genypterus maculatus Comp. Biochem. Physiol., B 88 1987 229 231
    • (1987) Comp. Biochem. Physiol., B , vol.88 , pp. 229-231
    • Carvajal, N.1    Kessi, E.2    Ainol, L.3
  • 13
    • 0027988841 scopus 로고
    • Subcellular localization, metal ion requirement and kinetic properties of arginase from the gill tissue of the bivalve Semele solida
    • N. Carvajal, E. Uribe, and C. Torres Subcellular localization, metal ion requirement and kinetic properties of arginase from the gill tissue of the bivalve Semele solida Comp. Biochem. Physiol., B 109 1994 683 689
    • (1994) Comp. Biochem. Physiol., B , vol.109 , pp. 683-689
    • Carvajal, N.1    Uribe, E.2    Torres, C.3
  • 15
    • 15244353301 scopus 로고    scopus 로고
    • Arginase: Structure, mechanism, and physiological role in male and female sexual arousal
    • D.W. Christianson Arginase: structure, mechanism, and physiological role in male and female sexual arousal Acc. Chem. Res. 38 2005 191 201
    • (2005) Acc. Chem. Res. , vol.38 , pp. 191-201
    • Christianson, D.W.1
  • 16
    • 0001545763 scopus 로고
    • Nitrogenous excretion
    • G.A. Kerkut L.I. Gilbert Comprehensive Insect Physiology Pergamon Press Oxford
    • D.G. Cochran Nitrogenous excretion G.A. Kerkut L.I. Gilbert Comprehensive Insect Physiology Biochemistry and Pharmacology vol. 4 1985 Pergamon Press Oxford 467 506
    • (1985) Biochemistry and Pharmacology , vol.4 , pp. 467-506
    • Cochran, D.G.1
  • 17
    • 0014781178 scopus 로고
    • Biochemical differentiation during amphibian metamorphosis
    • P.P. Cohen Biochemical differentiation during amphibian metamorphosis Science, Wash 168 1970 533 543
    • (1970) Science, Wash , vol.168 , pp. 533-543
    • Cohen, P.P.1
  • 18
    • 78651153791 scopus 로고
    • Disc electrophoresis. Method and application to human serum proteins
    • B.J. Davis Disc electrophoresis. Method and application to human serum proteins Ann. N. Y. Acad. Sci. 121 1964 404 427
    • (1964) Ann. N. Y. Acad. Sci. , vol.121 , pp. 404-427
    • Davis, B.J.1
  • 19
    • 26844505113 scopus 로고
    • Some kinetic properties of arginase isoenzymes during silkworm Bombyx mori ontogeny
    • M.A. Davtyan, T.G. Arutyunyan, M.A. Khachatyan, and A.R. Petrosyan Some kinetic properties of arginase isoenzymes during silkworm Bombyx mori ontogeny Biol. ZH. Arm. 34 1981 956 961
    • (1981) Biol. ZH. Arm. , vol.34 , pp. 956-961
    • Davtyan, M.A.1    Arutyunyan, T.G.2    Khachatyan, M.A.3    Petrosyan, A.R.4
  • 20
    • 12644315729 scopus 로고
    • Studies on the urea cycle of camel tick Hyalomma dromedarii during embryogenesis
    • A.S. Fahmy, S.A. Mohamed, and M.Y. Kamel Studies on the urea cycle of camel tick Hyalomma dromedarii during embryogenesis Egypt. J. Physiol. Sci. 18 1994 121 131
    • (1994) Egypt. J. Physiol. Sci. , vol.18 , pp. 121-131
    • Fahmy, A.S.1    Mohamed, S.A.2    Kamel, M.Y.3
  • 21
    • 12644268007 scopus 로고
    • Purification and characterization of arginase from eggs of the tick Hyalomma dromedarii
    • A.S. Fahmy, S.A. Mohamed, and M.Y. Kamel Purification and characterization of arginase from eggs of the tick Hyalomma dromedarii Egypt. J. Physiol. Sci. 18 1994 29 50
    • (1994) Egypt. J. Physiol. Sci. , vol.18 , pp. 29-50
    • Fahmy, A.S.1    Mohamed, S.A.2    Kamel, M.Y.3
  • 23
    • 0025127803 scopus 로고
    • Steady-state fluorescence and time-resolved fluorescence monitor changes in tryptophan environment in arginase from Saccharomyces cerevisiae upon removal of catalytic and structural metal ions
    • S.M. Green, J.R. Knutson, and P. Hensley Steady-state fluorescence and time-resolved fluorescence monitor changes in tryptophan environment in arginase from Saccharomyces cerevisiae upon removal of catalytic and structural metal ions Biochemistry 29 1990 9159 9168
    • (1990) Biochemistry , vol.29 , pp. 9159-9168
    • Green, S.M.1    Knutson, J.R.2    Hensley, P.3
  • 24
    • 0025790184 scopus 로고
    • Roles of metal ions in the maintenance of the tertiary and quaternary structure of arginase from Saccharomyces cerevisiae
    • S.M. Green, A. Ginsburg, M.S. Lewis, and P. Hensley Roles of metal ions in the maintenance of the tertiary and quaternary structure of arginase from Saccharomyces cerevisiae J. Biol. Chem. 266 1991 21,474 21,481
    • (1991) J. Biol. Chem. , vol.266 , pp. 21
    • Green, S.M.1    Ginsburg, A.2    Lewis, M.S.3    Hensley, P.4
  • 26
    • 0034824624 scopus 로고    scopus 로고
    • Biochemical analysis of arginase and ornithine carbamoyltransferase in human vitreous humor
    • M.F. Gursu Biochemical analysis of arginase and ornithine carbamoyltransferase in human vitreous humor Arch. Med. Res. 32 2001 432 435
    • (2001) Arch. Med. Res. , vol.32 , pp. 432-435
    • Gursu, M.F.1
  • 27
    • 0015238976 scopus 로고
    • Nuclear magnetic resonance studies of manganese binding of rat liver arginase
    • H. Hirsch-Kolb, H.J. Kolb, and D.M. Greenberg Nuclear magnetic resonance studies of manganese binding of rat liver arginase J. Biol. Chem. 246 1971 395 401
    • (1971) J. Biol. Chem. , vol.246 , pp. 395-401
    • Hirsch-Kolb, H.1    Kolb, H.J.2    Greenberg, D.M.3
  • 28
    • 0032964298 scopus 로고    scopus 로고
    • Identification of two arginase isoenzyme activities along the nephron of Meriones shawi
    • A. Hus-Citharel, and O. Levillain Identification of two arginase isoenzyme activities along the nephron of Meriones shawi Pflugers Arch. 437 1999 423 431
    • (1999) Pflugers Arch. , vol.437 , pp. 423-431
    • Hus-Citharel, A.1    Levillain, O.2
  • 29
    • 0343674479 scopus 로고
    • Purification and properties of gut arginase from earthworm Pheretima communissma
    • T. Iino, and T. Shimadate Purification and properties of gut arginase from earthworm Pheretima communissma Comp. Biochem. Physiol., B 83 1986 79 84
    • (1986) Comp. Biochem. Physiol., B , vol.83 , pp. 79-84
    • Iino, T.1    Shimadate, T.2
  • 31
    • 26844447218 scopus 로고
    • The ornithine-urea cycle in some parasitic helminths
    • P.A. Janssens, and C. Bryant The ornithine-urea cycle in some parasitic helminths Comp. Biochem. Physiol. 30 1969 261 269
    • (1969) Comp. Biochem. Physiol. , vol.30 , pp. 261-269
    • Janssens, P.A.1    Bryant, C.2
  • 33
    • 0015656354 scopus 로고
    • Purification and properties of arginase of rat kidney
    • G.A. Kaysen, and H.J. Strecker Purification and properties of arginase of rat kidney Biochem. J. 133 1973 779 788
    • (1973) Biochem. J. , vol.133 , pp. 779-788
    • Kaysen, G.A.1    Strecker, H.J.2
  • 34
    • 50549212331 scopus 로고
    • The regulation of some enzymes of intermediary metabolism-an introduction to enzyme physiology
    • W.E. Knox, and O. Greengard The regulation of some enzymes of intermediary metabolism-an introduction to enzyme physiology Adv. Enzyme Reg. 3 1965 247 313
    • (1965) Adv. Enzyme Reg. , vol.3 , pp. 247-313
    • Knox, W.E.1    Greengard, O.2
  • 35
    • 84941404091 scopus 로고
    • Untersuchungen über die Harnstoffbildung im Tierkörper
    • H.A. Krebs, and K. Henseleit Untersuchungen über die Harnstoffbildung im Tierkörper Z. Physiol. Chem. 210 1932 33 66
    • (1932) Z. Physiol. Chem. , vol.210 , pp. 33-66
    • Krebs, H.A.1    Henseleit, K.2
  • 36
    • 0015511802 scopus 로고
    • Lack of carbamoyl phosphate synthesis in some parasitic platyhelminths
    • B. Kurelec Lack of carbamoyl phosphate synthesis in some parasitic platyhelminths Comp. Biochem. Physiol., B 43 1972 769 780
    • (1972) Comp. Biochem. Physiol., B , vol.43 , pp. 769-780
    • Kurelec, B.1
  • 37
    • 0015975737 scopus 로고
    • Aspartate transearbamylase in some parasitic platyhelminths
    • B. Kurelec Aspartate transearbamylase in some parasitic platyhelminths Comp. Biochem. Physiol., B 47 1974 33 40
    • (1974) Comp. Biochem. Physiol., B , vol.47 , pp. 33-40
    • Kurelec, B.1
  • 38
    • 0016615087 scopus 로고
    • Catabolic path of arginine and NAD regeneration in the parasite Fasciola hepatica
    • B. Kurelec Catabolic path of arginine and NAD regeneration in the parasite Fasciola hepatica Comp. Biochem. Physiol., B 51 1975 151 156
    • (1975) Comp. Biochem. Physiol., B , vol.51 , pp. 151-156
    • Kurelec, B.1
  • 39
    • 0013968432 scopus 로고
    • Amino acid pool of the liver fluke (Fasciola hepatica L.)
    • B. Kurelec, and M. Rijavec Amino acid pool of the liver fluke (Fasciola hepatica L.) Comp. Biochem. Physiol. 19 1966 525 531
    • (1966) Comp. Biochem. Physiol. , vol.19 , pp. 525-531
    • Kurelec, B.1    Rijavec, M.2
  • 40
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head bacteriophage T4
    • U.K. Laemmli Cleavage of structural proteins during the assembly of the head bacteriophage T4 Nature 227 1970 680 685
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 42
    • 33751330608 scopus 로고
    • The determination of enzyme dissociation constants
    • H. Lineweaver, and D. Burk The determination of enzyme dissociation constants J. Am. Chem. Soc. 56 1934 658 666
    • (1934) J. Am. Chem. Soc. , vol.56 , pp. 658-666
    • Lineweaver, H.1    Burk, D.2
  • 44
    • 78651190784 scopus 로고
    • Automated and manual direct methods for the determination of blood urea
    • W.H. Marsh, B. Fingerhut, and H. Miller Automated and manual direct methods for the determination of blood urea Clin. Chem. 11 1965 624 627
    • (1965) Clin. Chem. , vol.11 , pp. 624-627
    • Marsh, W.H.1    Fingerhut, B.2    Miller, H.3
  • 45
    • 2442712483 scopus 로고    scopus 로고
    • Purification and characterization of Helicobacter pylori arginase, RocF: Unique features among the arginase superfamily
    • D.J. McGee, J. Zabaleta, R.J. Viator, T.L. Testeman, A.C. Ochoa, and G.L. Mendz Purification and characterization of Helicobacter pylori arginase, RocF: unique features among the arginase superfamily Eur. J. Biochem. 271 2004 1952 1962
    • (2004) Eur. J. Biochem. , vol.271 , pp. 1952-1962
    • McGee, D.J.1    Zabaleta, J.2    Viator, R.J.3    Testeman, T.L.4    Ochoa, A.C.5    Mendz, G.L.6
  • 46
    • 0027729290 scopus 로고
    • Eosinophil differentiation in response to Fasciola hepatica and its excreted/secreted antigens
    • E.A. Milbourne, and M.J. Howell Eosinophil differentiation in response to Fasciola hepatica and its excreted/secreted antigens Int. J. Parasitol. 23 1993 1005 1009
    • (1993) Int. J. Parasitol. , vol.23 , pp. 1005-1009
    • Milbourne, E.A.1    Howell, M.J.2
  • 47
    • 38949116073 scopus 로고
    • P.D. Boyer Academic Press New York
    • S.A. Mildvan P.D. Boyer The Enzymes vol. 2 1970 Academic Press New York 445 536
    • (1970) The Enzymes , vol.2 , pp. 445-536
    • Mildvan, S.A.1
  • 48
    • 0013799284 scopus 로고
    • Characteristics of arginase from ureotelic and nonureotelic animals
    • J. Mora, R. Tarrab, J. Martuscelli, and G. Soberon Characteristics of arginase from ureotelic and nonureotelic animals Biochem. J. 96 1965 588 594
    • (1965) Biochem. J. , vol.96 , pp. 588-594
    • Mora, J.1    Tarrab, R.2    Martuscelli, J.3    Soberon, G.4
  • 49
    • 0014012991 scopus 로고
    • On the structure and function of different arginases
    • J. Mora, R. Tarrab, and L.F. Bojalil On the structure and function of different arginases Biochim. Biophys. Acta 118 1966 206 209
    • (1966) Biochim. Biophys. Acta , vol.118 , pp. 206-209
    • Mora, J.1    Tarrab, R.2    Bojalil, L.F.3
  • 50
    • 0026575260 scopus 로고
    • Arginine catabolism in the phototrophic bacterium Rhodobacter capsulatus ELF1. Purification and properties of arginase
    • C. Moreno-Vivian, G. Soler, and F. Castillo Arginine catabolism in the phototrophic bacterium Rhodobacter capsulatus ELF1. Purification and properties of arginase Eur. J. Biochem. 204 1992 531 537
    • (1992) Eur. J. Biochem. , vol.204 , pp. 531-537
    • Moreno-Vivian, C.1    Soler, G.2    Castillo, F.3
  • 51
    • 14944367454 scopus 로고    scopus 로고
    • Structural metal dependency of the arginase from the human malaria parasite Plasmodium falciparum
    • I.B. Muller, R.D. Walter, and C. Wrenger Structural metal dependency of the arginase from the human malaria parasite Plasmodium falciparum Biol. Chem. 386 2005 117 126
    • (2005) Biol. Chem. , vol.386 , pp. 117-126
    • Muller, I.B.1    Walter, R.D.2    Wrenger, C.3
  • 52
    • 0023512859 scopus 로고
    • Immunohistochemical localization of arginase in human liver using monoclonal antibodies against human liver arginase
    • H. Multhaupt, P. Fritz, and K. Schumacher Immunohistochemical localization of arginase in human liver using monoclonal antibodies against human liver arginase Histochemistry 87 1987 465 470
    • (1987) Histochemistry , vol.87 , pp. 465-470
    • Multhaupt, H.1    Fritz, P.2    Schumacher, K.3
  • 53
    • 0026784019 scopus 로고
    • Presence of a partial urea cycle in the leech, Poecilobdella granulose
    • S. Natesan, B. Jayasundaramma, R. Ramamurthi, and S.R. Reddy Presence of a partial urea cycle in the leech, Poecilobdella granulose Experientia 48 1992 729 731
    • (1992) Experientia , vol.48 , pp. 729-731
    • Natesan, S.1    Jayasundaramma, B.2    Ramamurthi, R.3    Reddy, S.R.4
  • 54
    • 0016327986 scopus 로고
    • Structure and properties of arginase from the polychaete annelid Pista pacifica Berkeley
    • K.L. O'Malley, and R.C. Terwilliger Structure and properties of arginase from the polychaete annelid Pista pacifica Berkeley Biochem. J. 143 1974 591 597
    • (1974) Biochem. J. , vol.143 , pp. 591-597
    • O'Malley, K.L.1    Terwilliger, R.C.2
  • 55
    • 26844525110 scopus 로고
    • A reinvestigation of the status of the ornithine-urea cycle in adult Ascaris lumbricoides
    • R.W. Paltridge, and P.A. Janssens A reinvestigation of the status of the ornithine-urea cycle in adult Ascaris lumbricoides Comp. Biochem. Physiol., B 40 1971 503 513
    • (1971) Comp. Biochem. Physiol., B , vol.40 , pp. 503-513
    • Paltridge, R.W.1    Janssens, P.A.2
  • 56
    • 0017818947 scopus 로고
    • Is a urea cycle present in insects
    • R. Pant, and S. Kumar Is a urea cycle present in insects Biochem. J. 174 1978 341 344
    • (1978) Biochem. J. , vol.174 , pp. 341-344
    • Pant, R.1    Kumar, S.2
  • 57
    • 0015716863 scopus 로고
    • Different species of arginase in animal tissues
    • Z. Porembska Different species of arginase in animal tissues Enzyme 15 1973 198 209
    • (1973) Enzyme , vol.15 , pp. 198-209
    • Porembska, Z.1
  • 58
    • 0006034866 scopus 로고
    • Arginase activity in different fish species and tissues
    • T. Portugal, and A. Aksnes Arginase activity in different fish species and tissues Comp. Biochem. Physiol., B 76 1983 15 16
    • (1983) Comp. Biochem. Physiol., B , vol.76 , pp. 15-16
    • Portugal, T.1    Aksnes, A.2
  • 59
    • 0031472819 scopus 로고    scopus 로고
    • Purification and kinetic properties of Mus booduga (Gray) hepatic arginase
    • G.V. Prasad, V. okanatha, K. Sreekanth, and W. Rajendra Purification and kinetic properties of Mus booduga (Gray) hepatic arginase J. Enzyme Inhib. 12 1997 255 272
    • (1997) J. Enzyme Inhib. , vol.12 , pp. 255-272
    • Prasad, G.V.1    Okanatha, V.2    Sreekanth, K.3    Rajendra, W.4
  • 60
    • 0004819169 scopus 로고
    • Distribution of arginase and other ornithine cycle enzymes in the gut of the earthworm Lumbricus terrestris l., and some physiological and comparative implications
    • P. Prentø Distribution of arginase and other ornithine cycle enzymes in the gut of the earthworm Lumbricus terrestris l., and some physiological and comparative implications Comp. Biochem. Physiol., B 93 1989 509 515
    • (1989) Comp. Biochem. Physiol., B , vol.93 , pp. 509-515
    • Prentø, P.1
  • 61
    • 26844532124 scopus 로고
    • Arginine metabolism and interrelationships between the citric acid and urea cycle
    • W.D. McEleroy H.B. Glass Johns Hopkins Press Baltimore
    • S. Ratner Arginine metabolism and interrelationships between the citric acid and urea cycle W.D. McEleroy H.B. Glass Amino Acid Metabolism 1955 Johns Hopkins Press Baltimore 231 257
    • (1955) Amino Acid Metabolism , pp. 231-257
    • Ratner, S.1
  • 62
    • 26844515691 scopus 로고
    • EPR evidence for binuclear Mn(II) centers in rat liver arginase
    • R.S. Reczkowski, and D.E. Ash EPR evidence for binuclear Mn(II) centers in rat liver arginase J. Am. Chem. Soc. 114 1992 10,992 10,994
    • (1992) J. Am. Chem. Soc. , vol.114 , pp. 10
    • Reczkowski, R.S.1    Ash, D.E.2
  • 63
    • 0014407667 scopus 로고
    • A low molecular weight arginase in the earthworm
    • S.R.R. Reddy, and J.W. Campbell A low molecular weight arginase in the earthworm Biochim. Biophys. Acta 159 1968 557 560
    • (1968) Biochim. Biophys. Acta , vol.159 , pp. 557-560
    • Reddy, S.R.R.1    Campbell, J.W.2
  • 64
    • 15844409861 scopus 로고
    • Arginine metabolism in insect. Properties of insect fat body arginase
    • S.R.R. Reddy, and J.W. Campbell Arginine metabolism in insect. Properties of insect fat body arginase Comp. Biochem. Physiol. 28 1969 515 534
    • (1969) Comp. Biochem. Physiol. , vol.28 , pp. 515-534
    • Reddy, S.R.R.1    Campbell, J.W.2
  • 65
    • 15844421682 scopus 로고
    • Partial purification of bovine liver arginase
    • K.C. Robbins, and J. Shields Partial purification of bovine liver arginase Arch. Biochem. Biophys. 62 1956 55 62
    • (1956) Arch. Biochem. Biophys. , vol.62 , pp. 55-62
    • Robbins, K.C.1    Shields, J.2
  • 66
    • 0013850789 scopus 로고
    • Harnstoffzyklus bei einigen Rinderparasiten (Helminthen)
    • M. Rijavec, and B. Kurelec Harnstoffzyklus bei einigen Rinderparasiten (Helminthen) Z. Parasitenk 26 1965 168 172
    • (1965) Z. Parasitenk , vol.26 , pp. 168-172
    • Rijavec, M.1    Kurelec, B.2
  • 68
    • 0003831851 scopus 로고
    • Differential expressions of arginase in tissues by the fish Clarias batrachus L
    • R.A. Singh, and S.N. Singh Differential expressions of arginase in tissues by the fish Clarias batrachus L Biochem. Arch. 4 1988 381 390
    • (1988) Biochem. Arch. , vol.4 , pp. 381-390
    • Singh, R.A.1    Singh, S.N.2
  • 69
    • 0035693287 scopus 로고    scopus 로고
    • Allosteric inhibition of rat liver and kidney arginase by copper and mercury ions
    • C.D. Tormanen Allosteric inhibition of rat liver and kidney arginase by copper and mercury ions J. Enzym. Inhib. 16 2001 443 449
    • (2001) J. Enzym. Inhib. , vol.16 , pp. 443-449
    • Tormanen, C.D.1
  • 70
    • 0026524805 scopus 로고
    • Possible involvement of manganese in the catalytic mechanism of bovine liver arginase
    • S. Turkoglu, and I. Ozer Possible involvement of manganese in the catalytic mechanism of bovine liver arginase Int. J. Biochem. 24 1992 937 939
    • (1992) Int. J. Biochem. , vol.24 , pp. 937-939
    • Turkoglu, S.1    Ozer, I.2
  • 71
    • 0003959774 scopus 로고
    • Der N-Stoffwechsel der Aminosauren
    • G. der Tiere Fischer Verlag Stuttgart
    • K. Urich Der N-Stoffwechsel der Aminosauren G. der Tiere Vergleichende Biochemie 1990 Fischer Verlag Stuttgart 366 412
    • (1990) Vergleichende Biochemie , pp. 366-412
    • Urich, K.1
  • 72
    • 0033306728 scopus 로고    scopus 로고
    • Nitrogenous waste excretion by the larvae of a phylogenetically ancient vertebrate: The sea lamprey (Petromyzon marinus)
    • M.P. Wilkie, Y. Wang, P.J. Walsh, and J.Y. Youson Nitrogenous waste excretion by the larvae of a phylogenetically ancient vertebrate: the sea lamprey (Petromyzon marinus) Can. J. Zool. 77 1999 707 715
    • (1999) Can. J. Zool. , vol.77 , pp. 707-715
    • Wilkie, M.P.1    Wang, Y.2    Walsh, P.J.3    Youson, J.Y.4
  • 74
    • 0001315798 scopus 로고
    • Methylamine osmoregulatory solutes of elasmobranch fishes counteract urea inhibition of enzymes
    • P.H. Yancey, and G.N. Somero Methylamine osmoregulatory solutes of elasmobranch fishes counteract urea inhibition of enzymes J. Exp. Zool. 212 1980 205 213
    • (1980) J. Exp. Zool. , vol.212 , pp. 205-213
    • Yancey, P.H.1    Somero, G.N.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.