메뉴 건너뛰기




Volumn 19, Issue 1, 2000, Pages 22-29

Expression and purification of recombinant human indoleamine 2,3-dioxygenase

Author keywords

[No Author keywords available]

Indexed keywords

5 HYDROXYTRYPTOPHAN; ABSORPTION; AFFINITY CHROMATOGRAPHY; BACTERIUM CULTURE; CELLULOSE PHOSPHATE; CULTURE MEDIUM; ENZYME ACTIVITY; ENZYME PURIFICATION; ENZYME SUBSTRATE; ENZYME SYNTHESIS; ESCHERICHIA COLI; GENETIC STRAIN; HEMIN; HYBRID PROTEIN; INDOLEAMINE 2,3 DIOXYGENASE; RECOMBINANT ENZYME; TRYPTOPHAN;

EID: 0034045477     PISSN: 10465928     EISSN: None     Source Type: Journal    
DOI: 10.1006/prep.2000.1214     Document Type: Article
Times cited : (78)

References (47)
  • 1
    • 0005780874 scopus 로고
    • Indoleamine 2,3-dioxygenase: Properties and function of a superoxide utilizing enzyme
    • S. J. Lippard. New York: Wiley
    • Hayaishi O., Takikawa O., Yoshida R. Indoleamine 2,3-dioxygenase: Properties and function of a superoxide utilizing enzyme. Lippard S. J. Progress in Inorganic Chemistry-Bioinorganic Chemistry. 1990;75-95 Wiley, New York.
    • (1990) Progress in Inorganic Chemistry-Bioinorganic Chemistry , pp. 75-95
    • Hayaishi, O.1    Takikawa, O.2    Yoshida, R.3
  • 2
    • 0030341947 scopus 로고    scopus 로고
    • Metabolism and biology of tryptophan
    • G. F. Filippini, C. V. L. Costa, & A. Bertazzo. New York: Plenum Press
    • Brown R. Metabolism and biology of tryptophan. Filippini G. F., Costa C. V. L., Bertazzo A. Recent Advances in Tryptophan Research. 1996;15-25 Plenum Press, New York.
    • (1996) Recent Advances in Tryptophan Research , pp. 15-25
    • Brown, R.1
  • 3
    • 0023013615 scopus 로고
    • Tryptophan degradation in mice initiated by indoleamine 2,3-dioxygenase
    • Takikawa O., Yoshida R., Kido R., Hayaishi O. Tryptophan degradation in mice initiated by indoleamine 2,3-dioxygenase. J. Biol. Chem. 258:1986;3648-3653.
    • (1986) J. Biol. Chem. , vol.258 , pp. 3648-3653
    • Takikawa, O.1    Yoshida, R.2    Kido, R.3    Hayaishi, O.4
  • 4
    • 0018649875 scopus 로고
    • Induction of indoleamine 2,3-dioxygenase in mouse lung during virus infection
    • Yoshida R., Urade Y., Tokuda M., Hayaishi O. Induction of indoleamine 2,3-dioxygenase in mouse lung during virus infection. Proc. Natl. Acad. Sci. USA. 76:1979;4084-4086.
    • (1979) Proc. Natl. Acad. Sci. USA , vol.76 , pp. 4084-4086
    • Yoshida, R.1    Urade, Y.2    Tokuda, M.3    Hayaishi, O.4
  • 5
    • 0026035960 scopus 로고
    • Cerebral cortex and lung indoleamine 2,3-dioxygenase activity is increased in type-D retrovirus infected macaques
    • Saito K., Lankner A., Markey S. P., Heyes M. P. Cerebral cortex and lung indoleamine 2,3-dioxygenase activity is increased in type-D retrovirus infected macaques. Brain Res. 540:1991;353-356.
    • (1991) Brain Res. , vol.540 , pp. 353-356
    • Saito, K.1    Lankner, A.2    Markey, S.P.3    Heyes, M.P.4
  • 6
    • 0026663065 scopus 로고
    • Poliovirus induces indoleamine 2,3-dioxygenase and quinolinic acid synthesis in macaque brain
    • Heyes M. P., Saito K., Jacobowitz D., Markey S. P., Takikawa O., Vickers J. H. Poliovirus induces indoleamine 2,3-dioxygenase and quinolinic acid synthesis in macaque brain. FASEB J. 6:1992;2977-2989.
    • (1992) FASEB J. , vol.6 , pp. 2977-2989
    • Heyes, M.P.1    Saito, K.2    Jacobowitz, D.3    Markey, S.P.4    Takikawa, O.5    Vickers, J.H.6
  • 7
    • 0031920895 scopus 로고    scopus 로고
    • Altered tryptophan metabolism in mice with herpes simplex virus encephalitis: Increases in spinal cord quinolinic acid
    • Reinhard J. F. Jr. Altered tryptophan metabolism in mice with herpes simplex virus encephalitis: Increases in spinal cord quinolinic acid. Neurochem. Res. 23:1998;661-665.
    • (1998) Neurochem. Res. , vol.23 , pp. 661-665
    • Reinhard J.F., Jr.1
  • 8
    • 0018179447 scopus 로고
    • Induction of pulmonary indoleamine 2,3-dioxygenase by intraperitoneal injection of bacterial lipopolysaccharide
    • Yoshida R., Hayaishi O. Induction of pulmonary indoleamine 2,3-dioxygenase by intraperitoneal injection of bacterial lipopolysaccharide. Proc. Natl. Acad. Sci. USA. 75:1978;3998-4000.
    • (1978) Proc. Natl. Acad. Sci. USA , vol.75 , pp. 3998-4000
    • Yoshida, R.1    Hayaishi, O.2
  • 9
    • 0031908326 scopus 로고    scopus 로고
    • Dramatic changes in oxidative tryptophan metabolism along the kynurenine pathway in experimental cerebral and noncerebral malaria
    • Sanni L. A., Thomas S. R., Tattam B. N., Moore D. E., Chaudhri G., Stocker R., Hunt N. H. Dramatic changes in oxidative tryptophan metabolism along the kynurenine pathway in experimental cerebral and noncerebral malaria. Am. J. Pathol. 152:1998;611-619.
    • (1998) Am. J. Pathol. , vol.152 , pp. 611-619
    • Sanni, L.A.1    Thomas, S.R.2    Tattam, B.N.3    Moore, D.E.4    Chaudhri, G.5    Stocker, R.6    Hunt, N.H.7
  • 10
    • 0025101958 scopus 로고
    • IFN-γ is the inducer of indoleamine 2,3-dioxygenase in allografted tumor cells undergoing rejection
    • Takikawa O., Habara-Ohkubo A., Yoshida R. IFN-γ is the inducer of indoleamine 2,3-dioxygenase in allografted tumor cells undergoing rejection. J. Immunol. 145:1990;1246-1250.
    • (1990) J. Immunol. , vol.145 , pp. 1246-1250
    • Takikawa, O.1    Habara-Ohkubo, A.2    Yoshida, R.3
  • 11
    • 0026862474 scopus 로고
    • Oxidative tryptophan metabolism in renal allograft recipients: Increased kynurenine synthesis is associated with inflammation and OKT3 therapy
    • Holmes E. W., Russell P. M., Kinzler G. J., Reckard C. R., Flanigan R. C., Thompson D., Bermes E. W. Jr. Oxidative tryptophan metabolism in renal allograft recipients: Increased kynurenine synthesis is associated with inflammation and OKT3 therapy. Cytokine. 4:1992;205-213.
    • (1992) Cytokine , vol.4 , pp. 205-213
    • Holmes, E.W.1    Russell, P.M.2    Kinzler, G.J.3    Reckard, C.R.4    Flanigan, R.C.5    Thompson, D.6    Bermes E.W., Jr.7
  • 12
    • 0028967644 scopus 로고
    • The role of indoleamine 2,3-dioxygenase in the anti-tumor activity of human interferon-gamma in vivo
    • Burke F., Knowles R. G., East N., Balkwill F. R. The role of indoleamine 2,3-dioxygenase in the anti-tumor activity of human interferon-gamma in vivo. Int. J. Cancer. 60:1995;115-122.
    • (1995) Int. J. Cancer , vol.60 , pp. 115-122
    • Burke, F.1    Knowles, R.G.2    East, N.3    Balkwill, F.R.4
  • 13
    • 0032484538 scopus 로고    scopus 로고
    • Multiple molecular and cellular changes associated with tumour stasis and regression during IL-12 therapy of a murine breast cancer model
    • Dias S., Thomas H., Balkwill F. R. Multiple molecular and cellular changes associated with tumour stasis and regression during IL-12 therapy of a murine breast cancer model. Int. J. Cancer. 75:1998;151-157.
    • (1998) Int. J. Cancer , vol.75 , pp. 151-157
    • Dias, S.1    Thomas, H.2    Balkwill, F.R.3
  • 15
    • 0000056144 scopus 로고
    • Interferon blocks the growth of Toxoplasma gondii in human fibroblasts by inducing the host cells to degrade tryptophan
    • Pfefferkorn E. R. Interferon blocks the growth of Toxoplasma gondii in human fibroblasts by inducing the host cells to degrade tryptophan. Proc. Natl. Acad. Sci. USA. 81:1984;908-912.
    • (1984) Proc. Natl. Acad. Sci. USA , vol.81 , pp. 908-912
    • Pfefferkorn, E.R.1
  • 16
    • 0022475944 scopus 로고
    • Induction of tryptophan catabolism is the mechanism for gamma-interferon-mediated inhibition of intracellular Chlamydia psittaci replication in T24 cells
    • Byrne G. I., Lehmann L. K., Landry G. J. Induction of tryptophan catabolism is the mechanism for gamma-interferon-mediated inhibition of intracellular Chlamydia psittaci replication in T24 cells. Infect. Immun. 53:1986;347-351.
    • (1986) Infect. Immun. , vol.53 , pp. 347-351
    • Byrne, G.I.1    Lehmann, L.K.2    Landry, G.J.3
  • 17
    • 0023926018 scopus 로고
    • Mechanism of IFN-γ action: Characterization of indoleamine 2,3-dioxygenase in various human cells induced by IFN-γ And evaluation of the enzyme-mediated tryptophan degradation in its anticellular activity
    • Takikawa O., Kuroiwa T., Yamazaki F., Kido R. Mechanism of IFN-γ action: Characterization of indoleamine 2,3-dioxygenase in various human cells induced by IFN-γ and evaluation of the enzyme-mediated tryptophan degradation in its anticellular activity. J. Biol. Chem. 263:1988;2041-2048.
    • (1988) J. Biol. Chem. , vol.263 , pp. 2041-2048
    • Takikawa, O.1    Kuroiwa, T.2    Yamazaki, F.3    Kido, R.4
  • 18
    • 0040858936 scopus 로고
    • Induction of indoleamine 2,3-dioxygenase: A mechanism of the antitumor activity of interferon gamma
    • Ozaki Y., Edelstein M. P., Duch D. S. Induction of indoleamine 2,3-dioxygenase: A mechanism of the antitumor activity of interferon gamma. Proc. Natl. Acad. Sci. USA. 85:1988;1242-1246.
    • (1988) Proc. Natl. Acad. Sci. USA , vol.85 , pp. 1242-1246
    • Ozaki, Y.1    Edelstein, M.P.2    Duch, D.S.3
  • 19
    • 0023847864 scopus 로고
    • Dependence of the in vitro antiproliferative activity of recombinant human gamma-interferon on the concentration of tryptophan in culture media
    • de la Maza L. M., Peterson E. M. Dependence of the in vitro antiproliferative activity of recombinant human gamma-interferon on the concentration of tryptophan in culture media. Cancer Res. 48:1988;346-350.
    • (1988) Cancer Res. , vol.48 , pp. 346-350
    • De La Maza, L.M.1    Peterson, E.M.2
  • 20
    • 0031704905 scopus 로고    scopus 로고
    • Interferon-gamma-induced activation of indoleamine 2,3-dioxygenase in cord blood monocyte-derived macrophages inhibits the growth of group B streptococci
    • MacKenzie C. R., Hadding U., Daubener W. Interferon-gamma-induced activation of indoleamine 2,3-dioxygenase in cord blood monocyte-derived macrophages inhibits the growth of group B streptococci. J. Infect. Dis. 178:1998;875-878.
    • (1998) J. Infect. Dis. , vol.178 , pp. 875-878
    • MacKenzie, C.R.1    Hadding, U.2    Daubener, W.3
  • 21
    • 0033555723 scopus 로고    scopus 로고
    • Role of IFN-gamma-induced indoleamine 2,3 dioxygenase and inducible nitric oxide synthase in the replication of human cytomegalovirus in retinal pigment epithelial cells
    • Bodaghi B., Goureau O., Zipeto D., Laurent L., Virelizier J. L., Michelson S. Role of IFN-gamma-induced indoleamine 2,3 dioxygenase and inducible nitric oxide synthase in the replication of human cytomegalovirus in retinal pigment epithelial cells. J. Immunol. 162:1999;957-964.
    • (1999) J. Immunol. , vol.162 , pp. 957-964
    • Bodaghi, B.1    Goureau, O.2    Zipeto, D.3    Laurent, L.4    Virelizier, J.L.5    Michelson, S.6
  • 24
    • 0020702374 scopus 로고
    • Quinolinic acid: An endogenous metabolite can produce axon-sparing lesions in rat brain
    • Schwarcz R., Whestsell W. O., Mangano R. E. M. Quinolinic acid: An endogenous metabolite can produce axon-sparing lesions in rat brain. Science. 219:1983;316-318.
    • (1983) Science , vol.219 , pp. 316-318
    • Schwarcz, R.1    Whestsell, W.O.2    Mangano, R.E.M.3
  • 25
    • 0028839066 scopus 로고
    • Frontal cortex indoleamine 2,3-dioxygenase is increased in HIV-1-associated dementia
    • Sardar A. M., Reynolds G. P. Frontal cortex indoleamine 2,3-dioxygenase is increased in HIV-1-associated dementia. Neurosci. Lett. 187:1995;9-12.
    • (1995) Neurosci. Lett. , vol.187 , pp. 9-12
    • Sardar, A.M.1    Reynolds, G.P.2
  • 26
    • 0031468305 scopus 로고    scopus 로고
    • Kynurenine pathway inhibition reduces neurotoxicity of HIV-1-infected macrophages
    • Kerr S. J., Armati P. J., Pemberton L. A., Smythe G., Tattam B., Brew B. J. Kynurenine pathway inhibition reduces neurotoxicity of HIV-1-infected macrophages. Neurology. 49:1997;1671-1681.
    • (1997) Neurology , vol.49 , pp. 1671-1681
    • Kerr, S.J.1    Armati, P.J.2    Pemberton, L.A.3    Smythe, G.4    Tattam, B.5    Brew, B.J.6
  • 27
    • 0031748985 scopus 로고    scopus 로고
    • Sources of the neurotoxin quinolinic acid in the brain of HIV-1-infected patients and retrovirus-infected macaques
    • Heyes M. P., Saito K., Lackner A., Wiley C. A., Achim C. L., Markey S. P. Sources of the neurotoxin quinolinic acid in the brain of HIV-1-infected patients and retrovirus-infected macaques. FASEB J. 12:1998;881-896.
    • (1998) FASEB J. , vol.12 , pp. 881-896
    • Heyes, M.P.1    Saito, K.2    Lackner, A.3    Wiley, C.A.4    Achim, C.L.5    Markey, S.P.6
  • 28
    • 0030930823 scopus 로고    scopus 로고
    • Species heterogeneity between gerbils and rats: Quinolinate production by microglia and astrocytes and accumulations in response to ischemic brain injury and systemic immune activation
    • Heyes M. P., Saito K., Chen C. Y., Proescholdt M. G., Nowak T. S. Jr., Li J., Beagles K. E., Proescholdt M. A., Zito M. A., Kawai K., Markey S. P. Species heterogeneity between gerbils and rats: Quinolinate production by microglia and astrocytes and accumulations in response to ischemic brain injury and systemic immune activation. J. Neurochem. 69:1997;1519-1529.
    • (1997) J. Neurochem. , vol.69 , pp. 1519-1529
    • Heyes, M.P.1    Saito, K.2    Chen, C.Y.3    Proescholdt, M.G.4    Nowak T.S., Jr.5    Li, J.6    Beagles, K.E.7    Proescholdt, M.A.8    Zito, M.A.9    Kawai, K.10    Markey, S.P.11
  • 29
    • 0027459915 scopus 로고
    • Mechanism of delayed increases in kynurenine pathway metabolism in damaged brain regions following transient cerebral ischemia
    • Saito K., Nowak T. S. Jr., Markey S. P., Heyes M. P. Mechanism of delayed increases in kynurenine pathway metabolism in damaged brain regions following transient cerebral ischemia. J. Neurochem. 60:1993;180-192.
    • (1993) J. Neurochem. , vol.60 , pp. 180-192
    • Saito, K.1    Nowak T.S., Jr.2    Markey, S.P.3    Heyes, M.P.4
  • 30
    • 0029973593 scopus 로고    scopus 로고
    • Hydrogen peroxide-mediated neuronal cell death induced by an endogenous neurotoxin, 3-hydroxykynurenine
    • Okuda S., Nishiyama N., Saito H., Katsuki H. Hydrogen peroxide-mediated neuronal cell death induced by an endogenous neurotoxin, 3-hydroxykynurenine. Proc. Natl. Acad. Sci. USA. 93:1996;12553-12558.
    • (1996) Proc. Natl. Acad. Sci. USA , vol.93 , pp. 12553-12558
    • Okuda, S.1    Nishiyama, N.2    Saito, H.3    Katsuki, H.4
  • 31
    • 0026783169 scopus 로고
    • Increased brain concentrations of a neurotoxin, 3-hydroxykynurenine, in Huntington's disease
    • Pearson S. J., Reynolds G. P. Increased brain concentrations of a neurotoxin, 3-hydroxykynurenine, in Huntington's disease. Neurosci. Lett. 144:1992;199-201.
    • (1992) Neurosci. Lett. , vol.144 , pp. 199-201
    • Pearson, S.J.1    Reynolds, G.P.2
  • 32
    • 0031149920 scopus 로고    scopus 로고
    • Oxidation of products of 3-hydroxykynurenine bind to lens proteins: Relevance for nuclear cataract
    • Aquilina J. A., Carver J. A., Truscott R. J. W. Oxidation of products of 3-hydroxykynurenine bind to lens proteins: Relevance for nuclear cataract. Exp. Eye Res. 64:1997;727-735.
    • (1997) Exp. Eye Res. , vol.64 , pp. 727-735
    • Aquilina, J.A.1    Carver, J.A.2    Truscott, R.J.W.3
  • 33
    • 0021470843 scopus 로고
    • Inhibition of indoleamine 2,3-dioxygenase and tryptophan 2,3-dioxygenase by beta-carboline and indole derivatives
    • Eguchi N., Watanabe Y., Kawanishi K., Hashimoto Y., Hayaishi O. Inhibition of indoleamine 2,3-dioxygenase and tryptophan 2,3-dioxygenase by beta-carboline and indole derivatives. Arch. Biochem. Biophys. 232:1984;602-609.
    • (1984) Arch. Biochem. Biophys. , vol.232 , pp. 602-609
    • Eguchi, N.1    Watanabe, Y.2    Kawanishi, K.3    Hashimoto, Y.4    Hayaishi, O.5
  • 34
    • 0026347919 scopus 로고
    • 1-Methyl-dl-tryptophan, beta-(3-benzofuranyl)-dl-alanine (the oxygen analog of tryptophan), and beta-[3-benzo(b)thienyl]-dl-alanine (the sulfur analog of tryptophan) are competitive inhibitors for indoleamine 2,3-dioxygenase
    • Cady S. G., Sono M. 1-Methyl-dl-tryptophan, beta-(3-benzofuranyl)-dl-alanine (the oxygen analog of tryptophan), and beta-[3-benzo(b)thienyl]-dl-alanine (the sulfur analog of tryptophan) are competitive inhibitors for indoleamine 2,3-dioxygenase. Arch. Biochem. Biophys. 291:1991;326-333.
    • (1991) Arch. Biochem. Biophys. , vol.291 , pp. 326-333
    • Cady, S.G.1    Sono, M.2
  • 38
    • 0342974133 scopus 로고
    • Expression of human indoleamine 2,3-dioxygenase in E. coli
    • I. Ishiguro, R. Kido, T. Nagatsu, Y. Nagamura, & Y. Ohta. Toyoake: Fujita Health Univ. Press
    • Maeda H., Tone S., Kadoya A., Iwamonoto Y., Minatogawa Y., Kido R. Expression of human indoleamine 2,3-dioxygenase in E. coli. Ishiguro I., Kido R., Nagatsu T., Nagamura Y., Ohta Y. Advances in Tryptophan Research. 1992;417-420 Fujita Health Univ. Press, Toyoake.
    • (1992) Advances in Tryptophan Research , pp. 417-420
    • Maeda, H.1    Tone, S.2    Kadoya, A.3    Iwamonoto, Y.4    Minatogawa, Y.5    Kido, R.6
  • 39
    • 0023806075 scopus 로고
    • Single-step purification of polypeptides expressed in Escherichia coli as fusions with glutathione S-transferase
    • Smith D. B., Johnson K. S. Single-step purification of polypeptides expressed in Escherichia coli as fusions with glutathione S-transferase. Gene. 67:1988;31-40.
    • (1988) Gene , vol.67 , pp. 31-40
    • Smith, D.B.1    Johnson, K.S.2
  • 40
    • 0000448017 scopus 로고    scopus 로고
    • Single-step purification/solubilization of recombinant proteins: Applications to surfactant protein B
    • Holzinger A., Phillips K. S., Weaver T. E. Single-step purification/solubilization of recombinant proteins: Applications to surfactant protein B. Biotechniques. 20:1996;804-808.
    • (1996) Biotechniques , vol.20 , pp. 804-808
    • Holzinger, A.1    Phillips, K.S.2    Weaver, T.E.3
  • 42
    • 0016439201 scopus 로고
    • Isolation and characterisation of two outer membrane preparations from Escherichia coli
    • Mizushima S., Yamada H. Isolation and characterisation of two outer membrane preparations from Escherichia coli. Biochim. Biophys. Acta. 1975.
    • (1975) Biochim. Biophys. Acta
    • Mizushima, S.1    Yamada, H.2
  • 43
    • 29744466425 scopus 로고
    • Determination of serum proteins by means of the biuret reaction
    • Gornall A. G., Bardawill C. J., David M. M. Determination of serum proteins by means of the biuret reaction. J. Biol. Chem. 177:1949;751-766.
    • (1949) J. Biol. Chem. , vol.177 , pp. 751-766
    • Gornall, A.G.1    Bardawill, C.J.2    David, M.M.3
  • 44
    • 0026735580 scopus 로고
    • Nitric oxide synthase is a cytochrome P-450 type hemoprotein
    • White K. A., Marletta M. A. Nitric oxide synthase is a cytochrome P-450 type hemoprotein. Biochemistry. 28:1992;6627-6631.
    • (1992) Biochemistry , vol.28 , pp. 6627-6631
    • White, K.A.1    Marletta, M.A.2
  • 45
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli U. K. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature. 227:1970;680-685.
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 47
    • 0028601409 scopus 로고
    • Characterization of neural nitric oxide synthase and a C415H mutant, purified from a baculovirus overexpression system
    • Richards M. K., Marletta M. A. Characterization of neural nitric oxide synthase and a C415H mutant, purified from a baculovirus overexpression system. Biochemistry. 33:1994;14723-14732.
    • (1994) Biochemistry , vol.33 , pp. 14723-14732
    • Richards, M.K.1    Marletta, M.A.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.