메뉴 건너뛰기




Volumn 326, Issue 2, 2004, Pages 262-266

Microanalysis for MDR1 ATPase by high-performance liquid chromatography with a titanium dioxide column

Author keywords

ATPase; MDR1; Titanium dioxide column

Indexed keywords

CHROMATOGRAPHIC ANALYSIS; HIGH PERFORMANCE LIQUID CHROMATOGRAPHY; OXIDES; PURIFICATION; TITANIUM DIOXIDE;

EID: 10744227683     PISSN: 00032697     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.ab.2003.12.012     Document Type: Article
Times cited : (42)

References (23)
  • 1
    • 33645830172 scopus 로고
    • A surface glycoprotein modulating drug permeability in Chinese hamster ovary cell mutants
    • Juliano R.L., Ling V. A surface glycoprotein modulating drug permeability in Chinese hamster ovary cell mutants. Biochim. Biophys. Acta. 455:1976;152-162.
    • (1976) Biochim. Biophys. Acta , vol.455 , pp. 152-162
    • Juliano, R.L.1    Ling, V.2
  • 2
    • 0008632564 scopus 로고
    • Expression of a full-length cDNA for the human MDR1 gene confers resistance to colchicine, doxorubicin, and vinblastine
    • Ueda K., Cardarelli C., Gottesman M.M., Pastan I. Expression of a full-length cDNA for the human MDR1 gene confers resistance to colchicine, doxorubicin, and vinblastine. Proc. Natl. Acad. Sci. USA. 84:1987;3004-3008.
    • (1987) Proc. Natl. Acad. Sci. USA , vol.84 , pp. 3004-3008
    • Ueda, K.1    Cardarelli, C.2    Gottesman, M.M.3    Pastan, I.4
  • 6
    • 0033739725 scopus 로고    scopus 로고
    • Role of metabolic enzymes and efflux transporters in the absorption of drugs from the small intestine
    • Suzuki H., Sugiyama Y. Role of metabolic enzymes and efflux transporters in the absorption of drugs from the small intestine. Eur. J. Pharm. Sci. 12:2000;3-12.
    • (2000) Eur. J. Pharm. Sci. , vol.12 , pp. 3-12
    • Suzuki, H.1    Sugiyama, Y.2
  • 7
    • 0023874147 scopus 로고
    • A method for the determination of inorganic phosphate in the presence of labile organic phosphate and high concentrations of protein: Application to lens ATPases
    • Chifflet S., Torriglia A., Chiesa R., Tolosa S. A method for the determination of inorganic phosphate in the presence of labile organic phosphate and high concentrations of protein: application to lens ATPases. Anal. Biochem. 168:1988;1-4.
    • (1988) Anal. Biochem. , vol.168 , pp. 1-4
    • Chifflet, S.1    Torriglia, A.2    Chiesa, R.3    Tolosa, S.4
  • 8
    • 0035875760 scopus 로고    scopus 로고
    • A highly sensitive method for measurement of myosin ATPase activity by reversed-phase high-performance liquid chromatography
    • Samizo K., Ishikawa R., Nakamura A., Kohama K. A highly sensitive method for measurement of myosin ATPase activity by reversed-phase high-performance liquid chromatography. Anal. Biochem. 293:2001;212-215.
    • (2001) Anal. Biochem. , vol.293 , pp. 212-215
    • Samizo, K.1    Ishikawa, R.2    Nakamura, A.3    Kohama, K.4
  • 9
    • 0034617388 scopus 로고    scopus 로고
    • Assay of ATPase and Na,K-ATPase activity using high-performance liquid chromatographic determination of ADP derived from ATP
    • Sudo J., Terui J., Iwase H., Kakuno K. Assay of ATPase and Na,K-ATPase activity using high-performance liquid chromatographic determination of ADP derived from ATP. J. Chromatogr. B. Biomed. Sci. Appl. 744:2000;19-23.
    • (2000) J. Chromatogr. B. Biomed. Sci. Appl. , vol.744 , pp. 19-23
    • Sudo, J.1    Terui, J.2    Iwase, H.3    Kakuno, K.4
  • 10
    • 0037330645 scopus 로고    scopus 로고
    • Complete separation of adenine nucleotides for ATPase activity assay by ion-pair reversed-phase high-performance liquid chromatography
    • Ushimaru M., Fukushima Y. Complete separation of adenine nucleotides for ATPase activity assay by ion-pair reversed-phase high-performance liquid chromatography. Anal. Biochem. 313:2003;173-175.
    • (2003) Anal. Biochem. , vol.313 , pp. 173-175
    • Ushimaru, M.1    Fukushima, Y.2
  • 11
    • 85007894837 scopus 로고
    • New ceramic titania: Selective adsorbent for organic phosphates
    • Matsuda H., Nakamura H., Nakajima T. New ceramic titania: selective adsorbent for organic phosphates. Anal. Sci. 6:1990;911-912.
    • (1990) Anal. Sci. , vol.6 , pp. 911-912
    • Matsuda, H.1    Nakamura, H.2    Nakajima, T.3
  • 12
    • 0024362996 scopus 로고
    • P-glycoprotein gene (MDR1) cDNA from human adrenal: Normal P-glycoprotein carries Gly185 with an altered pattern of multidrug resistance
    • Kioka N., Tsubota J., Kakehi Y., Komano T., Gottesman M.M., Pastan I., Ueda K. P-glycoprotein gene (MDR1) cDNA from human adrenal: normal P-glycoprotein carries Gly185 with an altered pattern of multidrug resistance. Biochem. Biophys. Res. Commun. 162:1989;224-231.
    • (1989) Biochem. Biophys. Res. Commun. , vol.162 , pp. 224-231
    • Kioka, N.1    Tsubota, J.2    Kakehi, Y.3    Komano, T.4    Gottesman, M.M.5    Pastan, I.6    Ueda, K.7
  • 13
    • 0033520934 scopus 로고    scopus 로고
    • Large scale purification of detergent-soluble P-glycoprotein from Pichia pastoris cells and characterization of nucleotide binding properties of wild-type, Walker A, and Walker B mutant proteins
    • Lerner-Marmarosh N., Gimi K., Urbatsch I.L., Gros P., Senior A.E. Large scale purification of detergent-soluble P-glycoprotein from Pichia pastoris cells and characterization of nucleotide binding properties of wild-type, Walker A, and Walker B mutant proteins. J. Biol. Chem. 274:1999;34711-34718.
    • (1999) J. Biol. Chem. , vol.274 , pp. 34711-34718
    • Lerner-Marmarosh, N.1    Gimi, K.2    Urbatsch, I.L.3    Gros, P.4    Senior, A.E.5
  • 14
    • 0030848099 scopus 로고    scopus 로고
    • Purification of functional human P-glycoprotein expressed in Saccharomyces cerevisiae
    • Mao Q., Scarborough G.A. Purification of functional human P-glycoprotein expressed in Saccharomyces cerevisiae. Biochim. Biophys. Acta. 5:1997;107-118.
    • (1997) Biochim. Biophys. Acta , vol.5 , pp. 107-118
    • Mao, Q.1    Scarborough, G.A.2
  • 15
    • 0029100095 scopus 로고
    • Rapid purification of human P-glycoprotein mutants expressed transiently in HEK 293 cells by nickel-chelate chromatography and characterization of their drug-stimulated ATPase activities
    • Loo T.W., Clarke D.M. Rapid purification of human P-glycoprotein mutants expressed transiently in HEK 293 cells by nickel-chelate chromatography and characterization of their drug-stimulated ATPase activities. J. Biol. Chem. 270:1995;21449-21452.
    • (1995) J. Biol. Chem. , vol.270 , pp. 21449-21452
    • Loo, T.W.1    Clarke, D.M.2
  • 16
    • 0027482461 scopus 로고
    • Functional reconstitution of drug transport and ATPase activity in proteoliposomes containing partially purified P-glycoprotein
    • Sharom F.J., Yu X., Doige C.A. Functional reconstitution of drug transport and ATPase activity in proteoliposomes containing partially purified P-glycoprotein. J. Biol. Chem. 268:1993;24197-24202.
    • (1993) J. Biol. Chem. , vol.268 , pp. 24197-24202
    • Sharom, F.J.1    Yu, X.2    Doige, C.A.3
  • 17
    • 0028915094 scopus 로고
    • Purification and reconstitution of functional human P-glycoprotein
    • Ambudkar S.V. Purification and reconstitution of functional human P-glycoprotein. J. Bioenerg. Biomembr. 27:1995;23-29.
    • (1995) J. Bioenerg. Biomembr. , vol.27 , pp. 23-29
    • Ambudkar, S.V.1
  • 18
    • 0028362501 scopus 로고
    • Characterization of the ATPase activity of purified Chinese hamster P-glycoprotein
    • Urbatsch I.L., al-Shawi M.K., Senior A.E. Characterization of the ATPase activity of purified Chinese hamster P-glycoprotein. Biochemistry. 33:1994;7069-7076.
    • (1994) Biochemistry , vol.33 , pp. 7069-7076
    • Urbatsch, I.L.1    Al-Shawi, M.K.2    Senior, A.E.3
  • 20
    • 0026722467 scopus 로고
    • Expression of the human multidrug resistance cDNA in insect cells generates a high activity drug-stimulated membrane ATPase
    • Sarkadi B., Price E.M., Boucher R.C., Germann U.A., Scarborough G.A. Expression of the human multidrug resistance cDNA in insect cells generates a high activity drug-stimulated membrane ATPase. J. Biol. Chem. 267:1992;4854-4858.
    • (1992) J. Biol. Chem. , vol.267 , pp. 4854-4858
    • Sarkadi, B.1    Price, E.M.2    Boucher, R.C.3    Germann, U.A.4    Scarborough, G.A.5
  • 21
    • 0028953899 scopus 로고
    • Drug-stimulated ATPase activity of the human P-glycoprotein
    • Scarborough G.A. Drug-stimulated ATPase activity of the human P-glycoprotein. J. Bioenerg. Biomembr. 27:1995;37-41.
    • (1995) J. Bioenerg. Biomembr. , vol.27 , pp. 37-41
    • Scarborough, G.A.1
  • 22
    • 0041668155 scopus 로고    scopus 로고
    • The role of P-glycoprotein in intestinal tumorigenesis: Disruption of mdr1a suppresses polyp formation in Apc(Min/+) mice
    • Mochida Y., Taguchi K., Taniguchi S., Tsuneyoshi M., Kuwano H., Tsuzuki T., Kuwano M., Wada M. The role of P-glycoprotein in intestinal tumorigenesis: disruption of mdr1a suppresses polyp formation in Apc(Min/+) mice. Carcinogenesis. 24:2003;1219-1224.
    • (2003) Carcinogenesis , vol.24 , pp. 1219-1224
    • Mochida, Y.1    Taguchi, K.2    Taniguchi, S.3    Tsuneyoshi, M.4    Kuwano, H.5    Tsuzuki, T.6    Kuwano, M.7    Wada, M.8


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.