메뉴 건너뛰기




Volumn 1432, Issue 2, 1999, Pages 313-323

Interactive binding to the two principal ligand binding sites of human serum albumin: Effect of the neutral-to-base transition

Author keywords

Allosteric interaction; Displacement study; Human serum albumin; Ligand binding site; Neutral to base transition

Indexed keywords

ACENOCOUMAROL; ADIPIODONE; DIAZEPAM; HUMAN SERUM ALBUMIN; IBUPROFEN; PHENYLBUTAZONE;

EID: 0033045696     PISSN: 01674838     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0167-4838(99)00098-9     Document Type: Article
Times cited : (94)

References (31)
  • 1
    • 0020447370 scopus 로고
    • A comparative study of some physico-chemical properties of albumin samples from different sources - II. The characteristics of the N-B transition and the binding behavior with regard to warfarin and diazepam
    • Dröge J.H.M., Wilting J., Janssen L.H.M. A comparative study of some physico-chemical properties of albumin samples from different sources - II. The characteristics of the N-B transition and the binding behavior with regard to warfarin and diazepam. Biochem. Pharmacol. 31:1982;3781-3786.
    • (1982) Biochem. Pharmacol. , vol.31 , pp. 3781-3786
    • Dröge, J.H.M.1    Wilting, J.2    Janssen, L.H.M.3
  • 3
    • 0019538149 scopus 로고
    • Molecular aspects of ligand binding to serum albumin
    • Kragh-Hansen U. Molecular aspects of ligand binding to serum albumin. Pharmacol. Rev. 33:1981;17-53.
    • (1981) Pharmacol. Rev. , vol.33 , pp. 17-53
    • Kragh-Hansen, U.1
  • 4
    • 0021365056 scopus 로고
    • Nonenzymatic glycosylation of human serum albumin alters its conformation and function
    • Shaklai N., Garlick R.L., Bunn F. Nonenzymatic glycosylation of human serum albumin alters its conformation and function. J. Biol. Chem. 259:1984;3812-3817.
    • (1984) J. Biol. Chem. , vol.259 , pp. 3812-3817
    • Shaklai, N.1    Garlick, R.L.2    Bunn, F.3
  • 5
    • 0000278657 scopus 로고
    • A structural transformation in bovine and human plasma albumins in alkaline solution as revealed by rotary dispersion studies
    • Leonard W.J. Jr., Vijai K.K., Foster J.F. A structural transformation in bovine and human plasma albumins in alkaline solution as revealed by rotary dispersion studies. J. Biol. Chem. 283:1963;1984-1988.
    • (1963) J. Biol. Chem. , vol.283 , pp. 1984-1988
    • Leonard W.J., Jr.1    Vijai, K.K.2    Foster, J.F.3
  • 6
    • 0019223693 scopus 로고
    • Effect of albumin conformation on the binding of warfarin to human serum albumin on the hydrogen, calcium and chloride ion concentrations as studied by circular dichroism, fluorescence and equilibrium dialysis
    • Wilting J., van der Giesen W.F., Janssen L.H.M., Weideman M.M., Otagiri M., Perrin J.H. Effect of albumin conformation on the binding of warfarin to human serum albumin on the hydrogen, calcium and chloride ion concentrations as studied by circular dichroism, fluorescence and equilibrium dialysis. J. Biol. Chem. 255:1980;3032-3037.
    • (1980) J. Biol. Chem. , vol.255 , pp. 3032-3037
    • Wilting, J.1    Van Der Giesen, W.F.2    Janssen, L.H.M.3    Weideman, M.M.4    Otagiri, M.5    Perrin, J.H.6
  • 7
    • 0019159890 scopus 로고
    • The role of albumin conformation in the binding of diazepam to human serum albumin
    • Wilting J., Hart B.J., de Gier J.J. The role of albumin conformation in the binding of diazepam to human serum albumin. Biochim. Biophys. Acta. 626:1980;291-298.
    • (1980) Biochim. Biophys. Acta , vol.626 , pp. 291-298
    • Wilting, J.1    Hart, B.J.2    De Gier, J.J.3
  • 8
    • 0020362335 scopus 로고
    • The effects of N-B transition of human serum albumin on the specific drug binding sites
    • Wanwimolruk S., Birkett D.J. The effects of N-B transition of human serum albumin on the specific drug binding sites. Biochim. Biophys. Acta. 709:1982;247-255.
    • (1982) Biochim. Biophys. Acta , vol.709 , pp. 247-255
    • Wanwimolruk, S.1    Birkett, D.J.2
  • 10
    • 0031683467 scopus 로고    scopus 로고
    • Crystal structure of human serum albumin complexed with fatty acid reveals an asymmetric distribution of binding sites
    • Curry S., Mandelkow H., Brick P., Franks N. Crystal structure of human serum albumin complexed with fatty acid reveals an asymmetric distribution of binding sites. Nat. Struct. Biol. 5:1998;827-835.
    • (1998) Nat. Struct. Biol. , vol.5 , pp. 827-835
    • Curry, S.1    Mandelkow, H.2    Brick, P.3    Franks, N.4
  • 11
    • 0025050697 scopus 로고
    • Ceftriaxone binding to human serum albumin: Indirect displacement by probenecid and diazepam
    • McNamara P.J., Trueb V., Stoeckel K. Ceftriaxone binding to human serum albumin: indirect displacement by probenecid and diazepam. Biochem. Pharmacol. 40:1990;1247-1253.
    • (1990) Biochem. Pharmacol. , vol.40 , pp. 1247-1253
    • McNamara, P.J.1    Trueb, V.2    Stoeckel, K.3
  • 12
    • 0014216041 scopus 로고
    • Removal of fatty acids from serum albumin by charcoal treatment
    • Chen R.F. Removal of fatty acids from serum albumin by charcoal treatment. J. Biol. Chem. 242:1966;173-181.
    • (1966) J. Biol. Chem. , vol.242 , pp. 173-181
    • Chen, R.F.1
  • 14
    • 0019593952 scopus 로고
    • Fluorescence quenching studies with proteins
    • Eftink M.R., Ghiron C.A. Fluorescence quenching studies with proteins. Anal. Biochem. 114:1981;199-227.
    • (1981) Anal. Biochem. , vol.114 , pp. 199-227
    • Eftink, M.R.1    Ghiron, C.A.2
  • 15
  • 16
    • 0021984733 scopus 로고
    • Relations between high-affinity binding sites of markers for binding regions on albumin
    • Kragh-Hansen U. Relations between high-affinity binding sites of markers for binding regions on albumin. Biochem. J. 225:1985;629-638.
    • (1985) Biochem. J. , vol.225 , pp. 629-638
    • Kragh-Hansen, U.1
  • 17
    • 0024687284 scopus 로고
    • Role of coupling entropy in establishing the nature and magnitude of allosteric response
    • Reinhart G.D., Sharon S.B., Symcox M.M. Role of coupling entropy in establishing the nature and magnitude of allosteric response. Proc. Natl. Acad. Sci. USA. 86:1989;4032-4036.
    • (1989) Proc. Natl. Acad. Sci. USA , vol.86 , pp. 4032-4036
    • Reinhart, G.D.1    Sharon, S.B.2    Symcox, M.M.3
  • 18
    • 0016801988 scopus 로고
    • The characterization of two specific drug binding sites on human serum albumin
    • Sudlow G., Birkett D.J., Wade D.N. The characterization of two specific drug binding sites on human serum albumin. Mol. Pharmacol. 11:1975;824-832.
    • (1975) Mol. Pharmacol. , vol.11 , pp. 824-832
    • Sudlow, G.1    Birkett, D.J.2    Wade, D.N.3
  • 19
    • 0030592163 scopus 로고    scopus 로고
    • Characterization of site I on human serum albumin: Concept about the structure of a drug binding site
    • Yamasaki K., Maruyama T., Kragh-Hansen U., Otagiri M. Characterization of site I on human serum albumin: concept about the structure of a drug binding site. Biochim. Biophys. Acta. 1295:1996;147-157.
    • (1996) Biochim. Biophys. Acta , vol.1295 , pp. 147-157
    • Yamasaki, K.1    Maruyama, T.2    Kragh-Hansen, U.3    Otagiri, M.4
  • 21
    • 0028580070 scopus 로고
    • Characterization of region Ic in site I on human serum albumin: Microenviromental analysis using fluorescence spectroscopy
    • Yamasaki K., Miyoshi T., Maruyama T., Takadate A., Otagiri M. Characterization of region Ic in site I on human serum albumin: microenviromental analysis using fluorescence spectroscopy. Biol. Pharm. Bull. 17:1994;1656-1662.
    • (1994) Biol. Pharm. Bull. , vol.17 , pp. 1656-1662
    • Yamasaki, K.1    Miyoshi, T.2    Maruyama, T.3    Takadate, A.4    Otagiri, M.5
  • 22
    • 0024548387 scopus 로고
    • The molecular mechanism of the neutral-to-base transition of human serum albumin. Acid/base titration and proton nuclear magnetic resonance studies on a large peptic and a large tryptic fragment of albumin
    • Bos O.J.M., Labro J.F.A., Fischer M.J.E., Wilting J., Janssen L.H.M. The molecular mechanism of the neutral-to-base transition of human serum albumin. Acid/base titration and proton nuclear magnetic resonance studies on a large peptic and a large tryptic fragment of albumin. J. Biol. Chem. 264:1989;953-959.
    • (1989) J. Biol. Chem. , vol.264 , pp. 953-959
    • Bos, O.J.M.1    Labro, J.F.A.2    Fischer, M.J.E.3    Wilting, J.4    Janssen, L.H.M.5
  • 23
    • 0345681037 scopus 로고
    • Distances between Tyr-411 and Trp-214 of human serum albumin measured by fluorescence energy transfer: Effects of pH and fatty acids
    • Hagag N.G., Birnbaum E.R., Darnall D.W. Distances between Tyr-411 and Trp-214 of human serum albumin measured by fluorescence energy transfer: effects of pH and fatty acids. Fed. Proc. 41:1982;1189.
    • (1982) Fed. Proc. , vol.41 , pp. 1189
    • Hagag, N.G.1    Birnbaum, E.R.2    Darnall, D.W.3
  • 24
    • 0016759030 scopus 로고
    • Cooperativity in ligand binding: A new graphic analysis
    • De Meyts P., Roth J. Cooperativity in ligand binding: a new graphic analysis. Biochem. Biophys. Res. Commun. 66:1975;1118-1126.
    • (1975) Biochem. Biophys. Res. Commun. , vol.66 , pp. 1118-1126
    • De Meyts, P.1    Roth, J.2
  • 28
    • 0026749720 scopus 로고
    • Effect of albumin on adenylate cyclase receptor-related signal transduction of human peripheral blood mononuclear cells
    • Fischer M.J., van Oosterhout A.J.M., Janssen L.M.H., Nijkamp F.P. Effect of albumin on adenylate cyclase receptor-related signal transduction of human peripheral blood mononuclear cells. Biochem. Pharmacol. 44:1992;351-358.
    • (1992) Biochem. Pharmacol. , vol.44 , pp. 351-358
    • Fischer, M.J.1    Van Oosterhout, A.J.M.2    Janssen, L.M.H.3    Nijkamp, F.P.4
  • 29
    • 0020376406 scopus 로고
    • The kinetics of the binding of warfarin to human serum albumin as studied by stopped flow spectrophotometry
    • Wilting J., Kremer J.M.H., Izerman A.P., Schulman S.G. The kinetics of the binding of warfarin to human serum albumin as studied by stopped flow spectrophotometry. Biochim. Biophys. Acta. 706:1982;96-104.
    • (1982) Biochim. Biophys. Acta , vol.706 , pp. 96-104
    • Wilting, J.1    Kremer, J.M.H.2    Izerman, A.P.3    Schulman, S.G.4
  • 30
    • 0023916444 scopus 로고
    • Conformational change in plasma albumin due to interaction with isolated rat hepatocyte
    • Horie T., Mizuma T., Kasai S., Awazu S. Conformational change in plasma albumin due to interaction with isolated rat hepatocyte. Am. J. Physiol. 254:1988;G465-G470.
    • (1988) Am. J. Physiol. , vol.254
    • Horie, T.1    Mizuma, T.2    Kasai, S.3    Awazu, S.4
  • 31
    • 0027270167 scopus 로고
    • Steroid binding to human serum albumin and fragments thereof. Role of protein conformation and fatty acid content
    • Fischer M.J.E., Bos O.J.M., van der Linden R.F., Wilting J., Janssen L.H.M. Steroid binding to human serum albumin and fragments thereof. Role of protein conformation and fatty acid content. Biochem. Pharmacol. 45:1993;2411-2416.
    • (1993) Biochem. Pharmacol. , vol.45 , pp. 2411-2416
    • Fischer, M.J.E.1    Bos, O.J.M.2    Van Der Linden, R.F.3    Wilting, J.4    Janssen, L.H.M.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.