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Volumn 80, Issue 6, 2001, Pages 2898-2911

Detergents as probes of hydrophobic binding cavities in serum albumin and other water-soluble proteins

Author keywords

[No Author keywords available]

Indexed keywords

12 BROMODODECANOIC ACID; 7,8 DIBROMODODECYLMALTOSIDE; ALIPHATIC COMPOUND; BETA LACTOGLOBULIN; CARBOHYDRATE DERIVATIVE; DETERGENT; DODECYL SULFATE; DODECYLMALTOSIDE; FATTY ACID; LAURIC ACID; OVALBUMIN; PROTEIN; SERUM ALBUMIN; TRYPTOPHAN; UNCLASSIFIED DRUG; WATER;

EID: 0035022141     PISSN: 00063495     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0006-3495(01)76255-8     Document Type: Article
Times cited : (111)

References (65)
  • 3
    • 0004922287 scopus 로고
    • Disaggregation of the membrane protein cytochrome P450 by detergents
    • S. E. Harding, A. J. Rowe, and J. C. Horton, editors. Royal Society of Chemistry, London
    • Behlke, J. 1992. Disaggregation of the membrane protein cytochrome P450 by detergents. In Analytical Ultracentrifugation in Biochemistry and Polymer Science. S. E. Harding, A. J. Rowe, and J. C. Horton, editors. Royal Society of Chemistry, London. 485-494.
    • (1992) Analytical Ultracentrifugation in Biochemistry and Polymer Science , pp. 485-494
    • Behlke, J.1
  • 4
    • 0034634370 scopus 로고    scopus 로고
    • Crystallographic analysis reveals common modes of binding of medium and long-chain fatty acids to human serum albumin
    • Bhattacharya, A. A., T. Grüne, and S. Curry. 2000. Crystallographic analysis reveals common modes of binding of medium and long-chain fatty acids to human serum albumin. J. Mol. Biol. 303:721-732.
    • (2000) J. Mol. Biol. , vol.303 , pp. 721-732
    • Bhattacharya, A.A.1    Grüne, T.2    Curry, S.3
  • 5
    • 0025051457 scopus 로고
    • Quenching of tryptophan fluorescence by brominated phospholipid
    • Bolen, E. J., and P. W. Holloway. 1990. Quenching of tryptophan fluorescence by brominated phospholipid. Biochemistry. 29:9638-9643.
    • (1990) Biochemistry , vol.29 , pp. 9638-9643
    • Bolen, E.J.1    Holloway, P.W.2
  • 6
    • 0028227096 scopus 로고
    • Structure of serum albumin
    • Carter, D. C., and J. X. Ho. 1994. Structure of serum albumin. Adv. Protein Chem. 45:153-204.
    • (1994) Adv. Protein Chem. , vol.45 , pp. 153-204
    • Carter, D.C.1    Ho, J.X.2
  • 7
    • 0022914647 scopus 로고
    • Kinetic characterization of the normal and detergent-perturbed reaction cycles of the sarcoplasmic reticulum calcium pump
    • Champeil, P., M. le Maire, J. P. Andersen, F. Guillain, M. Gingold, S. Lund, and J. V. Møller. 1986. Kinetic characterization of the normal and detergent-perturbed reaction cycles of the sarcoplasmic reticulum calcium pump. J. Biol. Chem. 261:16372-16384.
    • (1986) J. Biol. Chem. , vol.261 , pp. 16372-16384
    • Champeil, P.1    Le Maire, M.2    Andersen, J.P.3    Guillain, F.4    Gingold, M.5    Lund, S.6    Møller, J.V.7
  • 8
    • 0014216041 scopus 로고
    • Removal of fatty acids from serum albumin by charcoal treatment
    • Chen, R. F. 1967. Removal of fatty acids from serum albumin by charcoal treatment. J. Biol. Chem. 242:173-181.
    • (1967) J. Biol. Chem. , vol.242 , pp. 173-181
    • Chen, R.F.1
  • 9
    • 0023655698 scopus 로고
    • Carbon 13 NMR studies of saturated fatty acids bound to bovine serum albumin. II. Electrostatic interactions in individual fatty acid binding sites
    • Cistola, D. P., D. M. Small, and J. A. Hamilton. 1987. Carbon 13 NMR studies of saturated fatty acids bound to bovine serum albumin. II. Electrostatic interactions in individual fatty acid binding sites. J. Biol. Chem. 262:10980-10985.
    • (1987) J. Biol. Chem. , vol.262 , pp. 10980-10985
    • Cistola, D.P.1    Small, D.M.2    Hamilton, J.A.3
  • 10
    • 0024294298 scopus 로고
    • Ionization and phase behaviour of fatty acids in water: Application of the Gibbs phase rule
    • Cistola, D. P., J. A. Hamilton, D. Jackson, and D. M. Small. 1988. Ionization and phase behaviour of fatty acids in water: application of the Gibbs phase rule. Biochemistry. 27:1881-1888.
    • (1988) Biochemistry , vol.27 , pp. 1881-1888
    • Cistola, D.P.1    Hamilton, J.A.2    Jackson, D.3    Small, D.M.4
  • 11
    • 0031683467 scopus 로고    scopus 로고
    • Crystal structure of human serum albumin complexed with fatty acid reveals an asymmetric distribution of binding sites
    • Curry, S., H. Mandelkow, P. Brick, and N. P. Franks. 1998. Crystal structure of human serum albumin complexed with fatty acid reveals an asymmetric distribution of binding sites. Nat. Struct. Biol. 5:827-835.
    • (1998) Nat. Struct. Biol. , vol.5 , pp. 827-835
    • Curry, S.1    Mandelkow, H.2    Brick, P.3    Franks, N.P.4
  • 12
    • 0032720125 scopus 로고    scopus 로고
    • Fatty acid binding to human serum albumin: New insight from crystallographic studies
    • Curry, S., P. Brick, and N. P. Franks. 1999. Fatty acid binding to human serum albumin: new insight from crystallographic studies. Biochim. Biophys. Acta. 1441:131-140.
    • (1999) Biochim. Biophys. Acta , vol.1441 , pp. 131-140
    • Curry, S.1    Brick, P.2    Franks, N.P.3
  • 13
    • 0032806293 scopus 로고    scopus 로고
    • Tryptophan octyl ester in detergent micelles of dodecylmaltoside: Fluorescence properties and quenching by brominated detergent analogs
    • de Foresta, B., J. Gallay, J. Sopkova, P. Champeil, and M. Vincent. 1999. Tryptophan octyl ester in detergent micelles of dodecylmaltoside: Fluorescence properties and quenching by brominated detergent analogs. Biophys. J. 77:3071-3084.
    • (1999) Biophys. J. , vol.77 , pp. 3071-3084
    • De Foresta, B.1    Gallay, J.2    Sopkova, J.3    Champeil, P.4    Vincent, M.5
  • 17
    • 0015528761 scopus 로고
    • Method for measuring the binding of small molecules to proteins from binding-induced alterations of physical-chemical properties
    • Halfman, C. J., and T. Nishida. 1972. Method for measuring the binding of small molecules to proteins from binding-induced alterations of physical-chemical properties. Biochemistry. 18:3493-3498.
    • (1972) Biochemistry , vol.18 , pp. 3493-3498
    • Halfman, C.J.1    Nishida, T.2
  • 18
    • 0025968147 scopus 로고
    • Locations of the three primary binding sites for long-chain fatty acids on bovine serum albumin
    • Hamilton, J. A., S. Era, S. P. Bhamidipati, and R. G. Reed. 1991. Locations of the three primary binding sites for long-chain fatty acids on bovine serum albumin. Proc. Natl. Acad. Sci. U.S.A. 88:2051-2054.
    • (1991) Proc. Natl. Acad. Sci. U.S.A. , vol.88 , pp. 2051-2054
    • Hamilton, J.A.1    Era, S.2    Bhamidipati, S.P.3    Reed, R.G.4
  • 19
    • 0026664548 scopus 로고
    • Atomic structure and chemistry of human serum albumin
    • He, X. M., and D. C. Carter. 1992. Atomic structure and chemistry of human serum albumin. Nature. 358:209-215.
    • (1992) Nature , vol.358 , pp. 209-215
    • He, X.M.A.1    Carter, D.C.2
  • 20
    • 0016657917 scopus 로고
    • Solubilization of membranes by detergents
    • Helenius, A., and K. Simons. 1975. Solubilization of membranes by detergents. Biochim. Biophys. Acta. 415:29-79.
    • (1975) Biochim. Biophys. Acta. , vol.415 , pp. 29-79
    • Helenius, A.1    Simons, K.2
  • 22
    • 0018462339 scopus 로고
    • Protein affinities for small molecules: Conceptions and misconceptions
    • Klotz, I. M., and D. L. Hunston. 1979. Protein affinities for small molecules: conceptions and misconceptions. Arch. Biochem. Biophys. 193:314-328.
    • (1979) Arch. Biochem. Biophys. , vol.193 , pp. 314-328
    • Klotz, I.M.1    Hunston, D.L.2
  • 23
    • 0023688913 scopus 로고
    • Evidence for a large and flexible region of human serum albumin possessing high affinity binding sites for salicylate, warfarin, and other ligands
    • Kragh-Hansen, U. 1988. Evidence for a large and flexible region of human serum albumin possessing high affinity binding sites for salicylate, warfarin, and other ligands. Mol. Pharmacol. 34:160-171.
    • (1988) Mol. Pharmacol. , vol.34 , pp. 160-171
    • Kragh-Hansen, U.1
  • 24
    • 0025378934 scopus 로고
    • Structure and ligand binding properties of human serum albumin
    • Kragh-Hansen, U. 1990. Structure and ligand binding properties of human serum albumin. Dan. Med. Bull. 37:57-84.
    • (1990) Dan. Med. Bull. , vol.37 , pp. 57-84
    • Kragh-Hansen, U.1
  • 25
    • 0016279797 scopus 로고
    • Protein binding of small molecules. IV. Relation between binding of phenolsulfophthalein dyes and other ligands with a high affinity for human serum albumin
    • Kragh-Hansen, U., J. V. Møller, and K. E. Lind. 1974. Protein binding of small molecules. IV. Relation between binding of phenolsulfophthalein dyes and other ligands with a high affinity for human serum albumin. Biochim. Biophys. Acta. 365:360-371.
    • (1974) Biochim. Biophys. Acta. , vol.365 , pp. 360-371
    • Kragh-Hansen, U.1    Møller, J.V.2    Lind, K.E.3
  • 26
    • 0027477920 scopus 로고
    • Transitional steps in the solubilization of protein-containing membranes and liposomes by non-ionic detergent
    • Kragh-Hansen, U., M. le Maire, J.-P. Noël, T. Gulik-Krzywicki, and J. V. Møller. 1993. Transitional steps in the solubilization of protein-containing membranes and liposomes by non-ionic detergent. Biochemistry. 32:1648-1656.
    • (1993) Biochemistry , vol.32 , pp. 1648-1656
    • Kragh-Hansen, U.1    Le Maire, M.2    Noël, J.-P.3    Gulik-Krzywicki, T.4    Møller, J.V.5
  • 27
    • 0031770290 scopus 로고    scopus 로고
    • The mechanism of detergent solubilization of liposomes and protein-containing membranes
    • Kragh-Hansen, U., M. le Maire, and J. V. Møller. 1998. The mechanism of detergent solubilization of liposomes and protein-containing membranes. Biophys. J. 75:2932-2946.
    • (1998) Biophys. J. , vol.75 , pp. 2932-2946
    • Kragh-Hansen, U.1    Le Maire, M.2    Møller, J.V.3
  • 28
    • 0027408611 scopus 로고
    • Quantitative analyses of the interaction between calcium ions and human serum albumin
    • Kragh-Hansen, U., and H. Vorum. 1993. Quantitative analyses of the interaction between calcium ions and human serum albumin. Clin. Chem. 39:202-208.
    • (1993) Clin. Chem. , vol.39 , pp. 202-208
    • Kragh-Hansen, U.1    Vorum, H.2
  • 29
    • 0029088548 scopus 로고
    • Interaction of detergents with lipid vesicles
    • Lasch, J. 1995. Interaction of detergents with lipid vesicles. Biochim. Biophys. Acta. 1241:269-292.
    • (1995) Biochim. Biophys. Acta. , vol.1241 , pp. 269-292
    • Lasch, J.1
  • 30
    • 0034707086 scopus 로고    scopus 로고
    • Interaction of membrane proteins and lipids with solubilizing detergent
    • le Maire, M., P. Champeil, and J. V. Møller. 2000. Interaction of membrane proteins and lipids with solubilizing detergent. Biochim. Biophys. Acta. 1508:86-111.
    • (2000) Biochim. Biophys. Acta , vol.1508 , pp. 86-111
    • Le Maire, M.1    Champeil, P.2    Møller, J.V.3
  • 31
    • 0023666958 scopus 로고
    • Binding of nonionic detergent to membranes: Flip-flop rate and location on the bilayer
    • le Maire, M., J. V. Møller, and P. Champeil. 1987. Binding of nonionic detergent to membranes: flip-flop rate and location on the bilayer. Biochemistry. 26:4803-4810.
    • (1987) Biochemistry , vol.26 , pp. 4803-4810
    • Le Maire, M.1    Møller, J.V.2    Champeil, P.3
  • 32
    • 0019210971 scopus 로고
    • Use of gel chromatography for determination of size and molecular weight of proteins: Further caution
    • le Maire, M., E. Rivas, and J. V. Møller. 1980. Use of gel chromatography for determination of size and molecular weight of proteins: further caution. Anal. Biochem. 106:12-21.
    • (1980) Anal. Biochem. , vol.106 , pp. 12-21
    • Le Maire, M.1    Rivas, E.2    Møller, J.V.3
  • 33
    • 0017082001 scopus 로고
    • Ligand-apomyoglobin interactions: Configurational adaptability of the haem binding site
    • Lind, K. E., and J. V. Møller. 1976. Ligand-apomyoglobin interactions: configurational adaptability of the haem binding site. Biochem. J. 155: 669-678.
    • (1976) Biochem. J. , vol.155 , pp. 669-678
    • Lind, K.E.1    Møller, J.V.2
  • 34
    • 0015839532 scopus 로고
    • The binding of deoxycholate and Triton X-100 to proteins
    • Makino, S., J. A. Reynolds, and C. Tanford. 1973. The binding of deoxycholate and Triton X-100 to proteins. J. Biol. Chem. 248:4926-4932.
    • (1973) J. Biol. Chem. , vol.248 , pp. 4926-4932
    • Makino, S.1    Reynolds, J.A.2    Tanford, C.3
  • 35
  • 40
    • 0032211227 scopus 로고    scopus 로고
    • Construction and use of a detergent-sensitive electrode to measure dodecyl sulfate activity and binding
    • Mokus, M., U. Kragh-Hansen, P. Letellier, M. le Maire, and J. V. Møller. 1998. Construction and use of a detergent-sensitive electrode to measure dodecyl sulfate activity and binding. Anal. Biochem. 264:34-40.
    • (1998) Anal. Biochem. , vol.264 , pp. 34-40
    • Mokus, M.1    Kragh-Hansen, U.2    Letellier, P.3    Le Maire, M.4    Møller, J.V.5
  • 42
    • 0000559797 scopus 로고
    • Uses of non-ionic and bile salt detergents in the study of membrane proteins
    • A. Watts and J. J. H. H. M. de Pont, editors. Elsevier Biochemical Press, Amsterdam
    • Møller, J. V., M. le Maire, and J. P. Andersen. 1986. Uses of non-ionic and bile salt detergents in the study of membrane proteins. In Progress in Protein-Lipid Interactions, Vol. 2. A. Watts and J. J. H. H. M. de Pont, editors. Elsevier Biochemical Press, Amsterdam. 147-176.
    • (1986) Progress in Protein-Lipid Interactions , vol.2 , pp. 147-176
    • Møller, J.V.1    Le Maire, M.2    Andersen, J.P.3
  • 43
    • 0017125145 scopus 로고
    • Use of gel chromatography for the determination of the Stokes radii of proteins in the presence and absence of detergents: A re-examination
    • Nozaki, Y., N. M. Schechter, J. A. Reynolds, and C. Tanford. 1976. Use of gel chromatography for the determination of the Stokes radii of proteins in the presence and absence of detergents: a re-examination. Biochemistry. 15:3884-3890.
    • (1976) Biochemistry , vol.15 , pp. 3884-3890
    • Nozaki, Y.1    Schechter, N.M.2    Reynolds, J.A.3    Tanford, C.4
  • 44
    • 0032083193 scopus 로고    scopus 로고
    • Effects of detergents on P-glycoprotein ATPase activitiy: Differences in perturbations of basal and verapamil-dependent activities
    • Orlowski, S., M.-A. Selosse, C. Boudon, C. Micoud, L. M. Mir, J. Belehradek, Jr., and M. Garrigos. 1998. Effects of detergents on P-glycoprotein ATPase activitiy: differences in perturbations of basal and verapamil-dependent activities. Cancer Biochem. Biophys. 16:85-111.
    • (1998) Cancer Biochem. Biophys. , vol.16 , pp. 85-111
    • Orlowski, S.1    Selosse, M.-A.2    Boudon, C.3    Micoud, C.4    Mir, L.M.5    Belehradek Jr., J.6    Garrigos, M.7
  • 45
    • 0022454690 scopus 로고
    • Laurate binding to human serum albumin: Multiple binding equilibria investigated by a dialysis exchange method
    • Pedersen, A. O., B. Hust, S. Andersen, F. Nielsen, and R. Brodersen. 1986. Laurate binding to human serum albumin: multiple binding equilibria investigated by a dialysis exchange method. Eur. J. Biochem. 154: 545-552.
    • (1986) Eur. J. Biochem. , vol.154 , pp. 545-552
    • Pedersen, A.O.1    Hust, B.2    Andersen, S.3    Nielsen, F.4    Brodersen, R.5
  • 46
    • 0028793377 scopus 로고
    • Effects of ionic strength and pH on the binding of medium chain fatty acids to human serum albumin
    • Pedersen, A. O., K. L. Mensberg, and U. Kragh-Hansen. 1995. Effects of ionic strength and pH on the binding of medium chain fatty acids to human serum albumin. Eur. J. Biochem. 233:395-405.
    • (1995) Eur. J. Biochem. , vol.233 , pp. 395-405
    • Pedersen, A.O.1    Mensberg, K.L.2    Kragh-Hansen, U.3
  • 48
    • 0031738305 scopus 로고    scopus 로고
    • 12-Bromododecanoic acid binds inside the calyx of bovine β-lactoglobulin
    • Qin, B. Y., L. K. Creamer, E. N. Baker, and G. B. Jameson. 1998. 12-Bromododecanoic acid binds inside the calyx of bovine β-lactoglobulin. FEBS Lett. 438:272-278.
    • (1998) FEBS Lett. , vol.438 , pp. 272-278
    • Qin, B.Y.1    Creamer, L.K.2    Baker, E.N.3    Jameson, G.B.4
  • 49
    • 0013934810 scopus 로고
    • Binding of large organic anions and neutral molecules by native bovine serum albumin
    • Ray, A., J. A. Reynolds, H. Polet, and J. Steinhardt. 1966. Binding of large organic anions and neutral molecules by native bovine serum albumin. Biochemistry. 5:2606-2616.
    • (1966) Biochemistry , vol.5 , pp. 2606-2616
    • Ray, A.1    Reynolds, J.A.2    Polet, H.3    Steinhardt, J.4
  • 50
    • 0023001023 scopus 로고
    • Location of long chain fatty acid-binding sites of bovine serum albumin by affinity labeling
    • Reed, R. G. 1986. Location of long chain fatty acid-binding sites of bovine serum albumin by affinity labeling. J. Biol. Chem. 261:15619-15624.
    • (1986) J. Biol. Chem. , vol.261 , pp. 15619-15624
    • Reed, R.G.1
  • 51
    • 0016724114 scopus 로고
    • Fragments of bovine serum albumin produced by limited proteolysis: Conformation and ligand binding
    • Reed, R. G., R. C. Feldhoff, O. L. Clute, and T. Peters, Jr. 1975. Fragments of bovine serum albumin produced by limited proteolysis: conformation and ligand binding. Biochemistry. 14:4578-4583.
    • (1975) Biochemistry , vol.14 , pp. 4578-4583
    • Reed, R.G.1    Feldhoff, R.C.2    Clute, O.L.3    Peters Jr., T.4
  • 52
    • 0017171791 scopus 로고
    • Fragments of bovine serum albumin produced by limited proteolysis: Complementary behavior of two large fragments
    • Reed, R. G., R. C. Feldhoff, and T. Peters, Jr. 1976. Fragments of bovine serum albumin produced by limited proteolysis: complementary behavior of two large fragments. Biochemistry. 15:5394-5398.
    • (1976) Biochemistry , vol.15 , pp. 5394-5398
    • Reed, R.G.1    Feldhoff, R.C.2    Peters Jr., T.3
  • 54
    • 0016691920 scopus 로고
    • Fatty acid binding to plasma albumin
    • Spector, A. A. 1975. Fatty acid binding to plasma albumin. J. Lipid Res. 16:165-179.
    • (1975) J. Lipid Res. , vol.16 , pp. 165-179
    • Spector, A.A.1
  • 56
    • 0015241501 scopus 로고
    • Differences between bovine and human serum albumins: Binding isotherms, optical rotatory dispersion, viscosity, hydrogen ion titration, and fluorescence effects
    • Steinhardt, J., J. Krijn, and J. G. Leidy. 1971. Differences between bovine and human serum albumins: binding isotherms, optical rotatory dispersion, viscosity, hydrogen ion titration, and fluorescence effects. Biochemistry. 10:4005-4015.
    • (1971) Biochemistry , vol.10 , pp. 4005-4015
    • Steinhardt, J.1    Krijn, J.2    Leidy, J.G.3
  • 57
    • 0016801988 scopus 로고
    • The characterization of two specific drug binding sites on human serum albumin
    • Sudlow, G., D. J. Birkett, and D. N. Wade. 1975. The characterization of two specific drug binding sites on human serum albumin. Mol. Pharmacol. 11:824-832.
    • (1975) Mol. Pharmacol. , vol.11 , pp. 824-832
    • Sudlow, G.1    Birkett, D.J.2    Wade, D.N.3
  • 58
    • 0017174391 scopus 로고
    • Further characterization of specific drug binding sites on human serum albumin
    • Sudlow, G., D. J. Birkett, and D. N. Wade. 1976. Further characterization of specific drug binding sites on human serum albumin. Mol. Pharmacol. 12:1052-1061.
    • (1976) Mol. Pharmacol. , vol.12 , pp. 1052-1061
    • Sudlow, G.1    Birkett, D.J.2    Wade, D.N.3
  • 59
    • 0019316305 scopus 로고
    • Binding of the Triton X series of nonionic surfactants to bovine serum albumin
    • Sukow, W. W., H. E. Sandberg, E. A. Lewis, D. J. Eatough, and L. D. Häuser. 1980. Binding of the Triton X series of nonionic surfactants to bovine serum albumin. Biochemistry. 19:912-917.
    • (1980) Biochemistry , vol.19 , pp. 912-917
    • Sukow, W.W.1    Sandberg, H.E.2    Lewis, E.A.3    Eatough, D.J.4    Häuser, L.D.5
  • 60
    • 0015505878 scopus 로고
    • Hydrophobic free energy, micelle formation and the association of proteins with amphiphiles
    • Tanford, C. 1972. Hydrophobic free energy, micelle formation and the association of proteins with amphiphiles. J. Mol. Biol. 67:59-74.
    • (1972) J. Mol. Biol. , vol.67 , pp. 59-74
    • Tanford, C.1
  • 62
    • 0017151703 scopus 로고
    • Characterization of membrane proteins in detergent solutions
    • Tanford, C., and J. A. Reynolds. 1976. Characterization of membrane proteins in detergent solutions. Biochim. Biophys. Acta. 457:133-170.
    • (1976) Biochim. Biophys. Acta. , vol.457 , pp. 133-170
    • Tanford, C.1    Reynolds, J.A.2
  • 63
    • 0026030046 scopus 로고
    • Binding of Triton X-100 to bovine serum albumin as studied by surface tension measurements
    • Tribout, M., S. Paredes, J. M. González-Manas, and F. M. Goñi. 1991. Binding of Triton X-100 to bovine serum albumin as studied by surface tension measurements. J. Biochem. Biophys. Methods. 22:129-133.
    • (1991) J. Biochem. Biophys. Methods. , vol.22 , pp. 129-133
    • Tribout, M.1    Paredes, S.2    González-Manas, J.M.3    Goñi, F.M.4
  • 64
    • 0018389587 scopus 로고
    • Protein-non-ionic detergent interaction
    • Wasylewski, Z., and A. Kozik. 1979. Protein-non-ionic detergent interaction. Eur. J. Biochem. 95:121-126.
    • (1979) Eur. J. Biochem. , vol.95 , pp. 121-126
    • Wasylewski, Z.1    Kozik, A.2
  • 65
    • 0030592163 scopus 로고    scopus 로고
    • Characterization of site I on human serum albumin: Concept about the structure of a drug binding site
    • Yamasaki, K., T. Maruyama, U. Kragh-Hansen, and M. Otagiri. 1996. Characterization of site I on human serum albumin: concept about the structure of a drug binding site. Biochim. Biophys. Acta. 1295:147-157.
    • (1996) Biochim. Biophys. Acta. , vol.1295 , pp. 147-157
    • Yamasaki, K.1    Maruyama, T.2    Kragh-Hansen, U.3    Otagiri, M.4


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