메뉴 건너뛰기




Volumn 62, Issue 10, 2014, Pages 2271-2283

Bioavailability and activity of natural food additive triterpenoids as influenced by protein

Author keywords

bovine serum albumin; circular dichroism; fluorescence; food additive; molecular modeling; triterpenoids

Indexed keywords

BIOCHEMISTRY; BODY FLUIDS; DICHROISM; DRUG PRODUCTS; FLUORESCENCE; FOOD ADDITIVES; FUNCTIONAL GROUPS; HYDROGEN BONDS; HYDROPHOBICITY; MAMMALS; MOLECULAR MODELING; PHYSIOLOGICAL MODELS; PROTEINS; THERMOANALYSIS; VAN DER WAALS FORCES; CARBOXYLIC ACIDS; GROUND STATE; SURFACE PLASMON RESONANCE;

EID: 84896345942     PISSN: 00218561     EISSN: 15205118     Source Type: Journal    
DOI: 10.1021/jf4049512     Document Type: Article
Times cited : (30)

References (62)
  • 1
    • 84861149095 scopus 로고    scopus 로고
    • Comparison of the triterpenoid content of berries and leaves of lingonberry Vaccinium vitis-idaea from Finland and Poland
    • Szakiel, A.; PaÌ̈czkowski, C.; Koivuniemi, H.; Huttunen, S. Comparison of the triterpenoid content of berries and leaves of lingonberry Vaccinium vitis-idaea from Finland and Poland J. Agric. Food Chem. 2012, 60, 4994-5002
    • (2012) J. Agric. Food Chem. , vol.60 , pp. 4994-5002
    • Szakiel, A.1    Paì̈czkowski, C.2    Koivuniemi, H.3    Huttunen, S.4
  • 2
    • 84874300079 scopus 로고
    • The chemistry of the triterpenes
    • Noller, C. R. The chemistry of the triterpenes Annu. Rev. Biochem. 1945, 14, 383-406
    • (1945) Annu. Rev. Biochem. , vol.14 , pp. 383-406
    • Noller, C.R.1
  • 3
    • 84876413596 scopus 로고    scopus 로고
    • Fruit cuticular waxes as a source of biologically active triterpenoids
    • Szakiel, A.; PaÌ̈czkowski, C.; Pensec, F.; Bertsch, C. Fruit cuticular waxes as a source of biologically active triterpenoids Phytochem. Rev. 2012, 11, 263-284
    • (2012) Phytochem. Rev. , vol.11 , pp. 263-284
    • Szakiel, A.1    Paì̈czkowski, C.2    Pensec, F.3    Bertsch, C.4
  • 6
    • 84880021398 scopus 로고    scopus 로고
    • Time course of pentacyclic triterpenoids from fruits and leaves of olive tree (Olea europaea L.) cv. Picual and cv. Cornezuelo during ripening
    • Peragón, J. Time course of pentacyclic triterpenoids from fruits and leaves of olive tree (Olea europaea L.) cv. Picual and cv. Cornezuelo during ripening J. Agric. Food Chem. 2013, 61, 6671-6678
    • (2013) J. Agric. Food Chem. , vol.61 , pp. 6671-6678
    • Peragón, J.1
  • 8
    • 84862803097 scopus 로고    scopus 로고
    • Anti-inflammatory activities of oleanolic acid on HMGB1 activated HUVECs
    • Yang, E.-J.; Lee, W.; Ku, S.-K.; Song, K.-S.; Bae, J.-S. Anti-inflammatory activities of oleanolic acid on HMGB1 activated HUVECs Food Chem. Toxicol. 2012, 50, 1288-1294
    • (2012) Food Chem. Toxicol. , vol.50 , pp. 1288-1294
    • Yang, E.-J.1    Lee, W.2    Ku, S.-K.3    Song, K.-S.4    Bae, J.-S.5
  • 9
    • 38949149637 scopus 로고    scopus 로고
    • Ursolic acid: An anti-and pro-inflammatory triterpenoid
    • Ikeda, Y.; Murakami, A.; Ohigashi, H. Ursolic acid: An anti-and pro-inflammatory triterpenoid Mol. Nutr. Food Res. 2008, 52, 26-42
    • (2008) Mol. Nutr. Food Res. , vol.52 , pp. 26-42
    • Ikeda, Y.1    Murakami, A.2    Ohigashi, H.3
  • 10
    • 84872769330 scopus 로고    scopus 로고
    • Ursane-type pentacyclic triterpenoids as useful platforms to discover anticancer drugs
    • Salvador, J. A. R.; Moreira, V. M.; Gonçalves, B. M. F.; Leal, A. S.; Jing, Y. K. Ursane-type pentacyclic triterpenoids as useful platforms to discover anticancer drugs Nat. Prod. Rep. 2012, 29, 1463-1479
    • (2012) Nat. Prod. Rep. , vol.29 , pp. 1463-1479
    • Salvador, J.A.R.1    Moreira, V.M.2    Gonçalves, B.M.F.3    Leal, A.S.4    Jing, Y.K.5
  • 11
    • 80055099463 scopus 로고    scopus 로고
    • Triggering of erythrocyte cell membrane scrambling by ursolic acid
    • Jilani, K.; Abed, M.; Zelenak, C.; Lang, E.; Qadri, S. M.; Lang, F. Triggering of erythrocyte cell membrane scrambling by ursolic acid J. Nat. Prod. 2011, 74, 2181-2186
    • (2011) J. Nat. Prod. , vol.74 , pp. 2181-2186
    • Jilani, K.1    Abed, M.2    Zelenak, C.3    Lang, E.4    Qadri, S.M.5    Lang, F.6
  • 13
    • 0019538149 scopus 로고
    • Molecular aspects of ligand binding to serum albumin
    • Kragh-Hansen, U. Molecular aspects of ligand binding to serum albumin Pharmacol. Rev. 1981, 33, 17-53
    • (1981) Pharmacol. Rev. , vol.33 , pp. 17-53
    • Kragh-Hansen, U.1
  • 14
    • 84858289984 scopus 로고    scopus 로고
    • Crystallographic survey of albumin drug interaction and preliminary applications in cancer chemotherapy
    • 7 th ed. Abraham, D. J. Rotella, D. P. John Wiley & Sons, Inc. Hoboken, NJ
    • Carter, D. C. Crystallographic survey of albumin drug interaction and preliminary applications in cancer chemotherapy. In Burger's Medicinal Chemistry, Drug Discovery, and Development, 7 th ed.; Abraham, D. J.; Rotella, D. P., Eds.; John Wiley & Sons, Inc.: Hoboken, NJ, 2010; pp 437-467.
    • (2010) Burger's Medicinal Chemistry, Drug Discovery, and Development , pp. 437-467
    • Carter, D.C.1
  • 16
    • 35148812430 scopus 로고    scopus 로고
    • Interstitial flow and its effects in soft tissues
    • Swartz, M. A.; Fleury, M. E. Interstitial flow and its effects in soft tissues Annu. Rev. Biomed. Eng. 2007, 9, 229-256
    • (2007) Annu. Rev. Biomed. Eng. , vol.9 , pp. 229-256
    • Swartz, M.A.1    Fleury, M.E.2
  • 18
    • 0014511903 scopus 로고
    • Optical studies of drug-protein complexes. II. Interaction of phenylbutazone and its analogues with human serum albumin
    • Chignell, C. F. Optical studies of drug-protein complexes. II. Interaction of phenylbutazone and its analogues with human serum albumin Mol. Pharmacol. 1969, 5, 244-252
    • (1969) Mol. Pharmacol. , vol.5 , pp. 244-252
    • Chignell, C.F.1
  • 19
    • 34247279859 scopus 로고    scopus 로고
    • Supramolecular photochirogenesis with biomolecules. Mechanistic studies on the enantiodifferentiation for the photocyclodimerization of 2-anthracenecarboxylate mediated by bovine serum albumin
    • Nishijima, M.; Pace, T. C. S.; Nakamura, A.; Mori, T.; Wada, T.; Bohne, C.; Inoue, Y. Supramolecular photochirogenesis with biomolecules. Mechanistic studies on the enantiodifferentiation for the photocyclodimerization of 2-anthracenecarboxylate mediated by bovine serum albumin J. Org. Chem. 2007, 72, 2707-2715
    • (2007) J. Org. Chem. , vol.72 , pp. 2707-2715
    • Nishijima, M.1    Pace, T.C.S.2    Nakamura, A.3    Mori, T.4    Wada, T.5    Bohne, C.6    Inoue, Y.7
  • 20
    • 1642546383 scopus 로고    scopus 로고
    • Computation and analysis of protein circular dichroism spectra
    • Sreerama, N.; Woody, R. W. Computation and analysis of protein circular dichroism spectra Methods Enzymol. 2004, 383, 318-351
    • (2004) Methods Enzymol. , vol.383 , pp. 318-351
    • Sreerama, N.1    Woody, R.W.2
  • 21
    • 77953865084 scopus 로고    scopus 로고
    • 3 rd ed. Springer Science+Business Media: New York, NY
    • Lakowicz, J. R. Principles of Fluorescence Spectroscopy, 3 rd ed.; Springer Science+Business Media: New York, NY, 2006; pp 63-351.
    • (2006) Principles of Fluorescence Spectroscopy , pp. 63-351
    • Lakowicz, J.R.1
  • 22
    • 84874420195 scopus 로고    scopus 로고
    • Binding of hydroxyquinoline probes to human serum albumin: Combining molecular modeling and Förster's resonance energy transfer spectroscopy to understand flexible ligand binding
    • Abou-Zied, O. K.; Al-Lawatia, N.; Elstner, M.; Steinbrecher, T. B. Binding of hydroxyquinoline probes to human serum albumin: Combining molecular modeling and Förster's resonance energy transfer spectroscopy to understand flexible ligand binding J. Phys. Chem. B 2013, 117, 1062-1074
    • (2013) J. Phys. Chem. B , vol.117 , pp. 1062-1074
    • Abou-Zied, O.K.1    Al-Lawatia, N.2    Elstner, M.3    Steinbrecher, T.B.4
  • 24
    • 84866661019 scopus 로고    scopus 로고
    • Structures of bovine, equine and leporine serum albumin
    • Bujacz, A. Structures of bovine, equine and leporine serum albumin Acta Crystallogr., Sect. D: Biol. Crystallogr. 2012, 68, 1278-1289
    • (2012) Acta Crystallogr., Sect. D: Biol. Crystallogr. , vol.68 , pp. 1278-1289
    • Bujacz, A.1
  • 25
    • 84879997821 scopus 로고    scopus 로고
    • Crystallographic studies of the complexes of bovine and equine serum albumin with 3,5-diiodosalicylic acid
    • Sekula, B.; Zielinski, K.; Bujacz, A. Crystallographic studies of the complexes of bovine and equine serum albumin with 3,5-diiodosalicylic acid Int. J. Biol. Macromol. 2013, 60, 316-324
    • (2013) Int. J. Biol. Macromol. , vol.60 , pp. 316-324
    • Sekula, B.1    Zielinski, K.2    Bujacz, A.3
  • 28
    • 0542406372 scopus 로고
    • Very strong hydrogen bonding
    • Emsley, J. Very strong hydrogen bonding Chem. Soc. Rev. 1980, 9, 91-124
    • (1980) Chem. Soc. Rev. , vol.9 , pp. 91-124
    • Emsley, J.1
  • 29
    • 0030632978 scopus 로고    scopus 로고
    • "Strong" hydrogen bonds in chemistry and biology
    • Perrin, C. L.; Nielson, J. B. "Strong" hydrogen bonds in chemistry and biology Annu. Rev. Phys. Chem. 1997, 48, 511-544
    • (1997) Annu. Rev. Phys. Chem. , vol.48 , pp. 511-544
    • Perrin, C.L.1    Nielson, J.B.2
  • 31
    • 77649184736 scopus 로고    scopus 로고
    • Oleanolic acid and ursolic acid induce apoptosis in four human liver cancer cell lines
    • Yan, S.-l.; Huang, C.-y.; Wu, S.-t.; Yin, M.-c. Oleanolic acid and ursolic acid induce apoptosis in four human liver cancer cell lines Toxicol. In Vitro 2010, 24, 842-848
    • (2010) Toxicol. in Vitro , vol.24 , pp. 842-848
    • Yan, S.-L.1    Huang, C.-Y.2    Wu, S.-T.3    Yin, M.-C.4
  • 32
    • 84881323608 scopus 로고    scopus 로고
    • A fluorescence spectroscopic study of the interaction between Glipizide and bovine serum albumin and its analytical application
    • Cao, S. N.; Liu, B. S.; Li, Z. Y.; Chong, B. H. A fluorescence spectroscopic study of the interaction between Glipizide and bovine serum albumin and its analytical application J. Lumin. 2014, 145, 94-99
    • (2014) J. Lumin. , vol.145 , pp. 94-99
    • Cao, S.N.1    Liu, B.S.2    Li, Z.Y.3    Chong, B.H.4
  • 33
    • 84873453386 scopus 로고    scopus 로고
    • Binding sites of resveratrol, genistein, and curcumin with milk α -and β -caseins
    • Bourassa, P.; Bariyanga, J.; Tajmir-Riahi, H. A. Binding sites of resveratrol, genistein, and curcumin with milk α-and β -caseins J. Phys. Chem. B 2013, 117, 1287-1295
    • (2013) J. Phys. Chem. B , vol.117 , pp. 1287-1295
    • Bourassa, P.1    Bariyanga, J.2    Tajmir-Riahi, H.A.3
  • 34
    • 84855850311 scopus 로고    scopus 로고
    • Impact of albumin on drug delivery -New applications on the horizon
    • Elsadek, B.; Kratz, F. Impact of albumin on drug delivery-New applications on the horizon J. Controlled Release 2012, 157, 4-28
    • (2012) J. Controlled Release , vol.157 , pp. 4-28
    • Elsadek, B.1    Kratz, F.2
  • 35
    • 84862702122 scopus 로고    scopus 로고
    • Clinical impact of serum proteins on drug delivery
    • Kratz, F.; Elsadek, B. Clinical impact of serum proteins on drug delivery J. Controlled Release 2012, 161, 429-445
    • (2012) J. Controlled Release , vol.161 , pp. 429-445
    • Kratz, F.1    Elsadek, B.2
  • 36
    • 11844253806 scopus 로고    scopus 로고
    • Flavonoid-serum albumin complexation: Determination of binding constants and binding sites by fluorescence spectroscopy
    • Dufour, C.; Dangles, O. Flavonoid-serum albumin complexation: determination of binding constants and binding sites by fluorescence spectroscopy Biochim. Biophys. Acta, Gen. Subj. 2005, 1721, 164-173
    • (2005) Biochim. Biophys. Acta, Gen. Subj. , vol.1721 , pp. 164-173
    • Dufour, C.1    Dangles, O.2
  • 37
    • 34447556028 scopus 로고    scopus 로고
    • Binding of bioactive phytochemical piperine with human serum albumin: A spectrofluorometric study
    • Suresh, D. V.; Mahesha, H. G.; Rao, A. G. A.; Srinivasan, K. Binding of bioactive phytochemical piperine with human serum albumin: A spectrofluorometric study Biopolymers 2007, 86, 265-275
    • (2007) Biopolymers , vol.86 , pp. 265-275
    • Suresh, D.V.1    Mahesha, H.G.2    Rao, A.G.A.3    Srinivasan, K.4
  • 38
    • 80052316719 scopus 로고    scopus 로고
    • Dansyl labeling to modulate the relative affinity of bile acids for the binding sites of human serum albumin
    • Rohacova, J.; Sastre, G.; Marin, M. L.; Miranda, M. A. Dansyl labeling to modulate the relative affinity of bile acids for the binding sites of human serum albumin J. Phys. Chem. B 2011, 115, 10518-10524
    • (2011) J. Phys. Chem. B , vol.115 , pp. 10518-10524
    • Rohacova, J.1    Sastre, G.2    Marin, M.L.3    Miranda, M.A.4
  • 39
    • 79551470966 scopus 로고    scopus 로고
    • Exploring the drug-binding site Sudlow i of human serum albumin: The role of water and Trp214 in molecular recognition and ligand binding
    • Abou-Zied, O. K.; Al-Lawatia, N. Exploring the drug-binding site Sudlow I of human serum albumin: The role of water and Trp214 in molecular recognition and ligand binding ChemPhysChem 2011, 12, 270-274
    • (2011) ChemPhysChem , vol.12 , pp. 270-274
    • Abou-Zied, O.K.1    Al-Lawatia, N.2
  • 41
    • 84855837542 scopus 로고    scopus 로고
    • Locating the binding sites of folic acid with milk α -and β -caseins
    • Bourassa, P.; Tajmir-Riahi, H. A. Locating the binding sites of folic acid with milk α-and β -caseins J. Phys. Chem. B 2012, 116, 513-519
    • (2012) J. Phys. Chem. B , vol.116 , pp. 513-519
    • Bourassa, P.1    Tajmir-Riahi, H.A.2
  • 42
    • 30344458801 scopus 로고    scopus 로고
    • Determination of oleanolic acid in human plasma and study of its pharmacokinetics in Chinese healthy male volunteers by HPLC tandem mass spectrometry
    • Song, M.; Hang, T.-j.; Wang, Y.; Jiang, L.; Wu, X.-l. Determination of oleanolic acid in human plasma and study of its pharmacokinetics in Chinese healthy male volunteers by HPLC tandem mass spectrometry J. Pharm. Biomed. Anal. 2006, 40, 190-196
    • (2006) J. Pharm. Biomed. Anal. , vol.40 , pp. 190-196
    • Song, M.1    Hang, T.-J.2    Wang, Y.3    Jiang, L.4    Wu, X.-L.5
  • 43
    • 78651252487 scopus 로고    scopus 로고
    • Quantitation of ursolic acid in human plasma by ultra performance liquid chromatography tandem mass spectrometry and its pharmacokinetic study
    • Xia, Y. Y.; Wei, G. L.; Si, D. Y.; Liu, C. X. Quantitation of ursolic acid in human plasma by ultra performance liquid chromatography tandem mass spectrometry and its pharmacokinetic study J. Chromatogr. B: Biomed. Sci. Appl. 2011, 879, 219-224
    • (2011) J. Chromatogr. B: Biomed. Sci. Appl. , vol.879 , pp. 219-224
    • Xia, Y.Y.1    Wei, G.L.2    Si, D.Y.3    Liu, C.X.4
  • 44
    • 79954422847 scopus 로고    scopus 로고
    • Development of a liquid chromatography-mass spectrometry method for the determination of ursolic acid in rat plasma and tissue: Application to the pharmacokinetic and tissue distribution study
    • Chen, Q. H.; Luo, S. W.; Zhang, Y. L.; Chen, Z. L. Development of a liquid chromatography-mass spectrometry method for the determination of ursolic acid in rat plasma and tissue: Application to the pharmacokinetic and tissue distribution study Anal. Bioanal. Chem. 2011, 399, 2877-2884
    • (2011) Anal. Bioanal. Chem. , vol.399 , pp. 2877-2884
    • Chen, Q.H.1    Luo, S.W.2    Zhang, Y.L.3    Chen, Z.L.4
  • 45
    • 84864687685 scopus 로고    scopus 로고
    • Bioavailability, distribution, and antioxidative effects of selected triterpenes in mice
    • Yin, M.-C.; Lin, M.-C.; Mong, M.-C.; Lin, C.-Y. Bioavailability, distribution, and antioxidative effects of selected triterpenes in mice J. Agric. Food Chem. 2012, 60, 7697-7701
    • (2012) J. Agric. Food Chem. , vol.60 , pp. 7697-7701
    • Yin, M.-C.1    Lin, M.-C.2    Mong, M.-C.3    Lin, C.-Y.4
  • 46
    • 0017820499 scopus 로고
    • Thermodynamic analysis of ion effects on the binding and conformational equilibria of proteins and nucleic acids: The roles of ion association or release, screening, and ion effects on water activity
    • Record, M. T., Jr.; Anderson, C. F.; Lohman, T. M. Thermodynamic analysis of ion effects on the binding and conformational equilibria of proteins and nucleic acids: the roles of ion association or release, screening, and ion effects on water activity Q. Rev. Biophys. 1978, 11, 103-178
    • (1978) Q. Rev. Biophys. , vol.11 , pp. 103-178
    • Record, Jr.M.T.1    Anderson, C.F.2    Lohman, T.M.3
  • 47
    • 0019889063 scopus 로고
    • Thermodynamics of protein association reactions: Forces contributing to stability
    • Ross, P. D.; Subramanian, S. Thermodynamics of protein association reactions: Forces contributing to stability Biochemistry 1981, 20, 3096-3102
    • (1981) Biochemistry , vol.20 , pp. 3096-3102
    • Ross, P.D.1    Subramanian, S.2
  • 48
    • 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. 1975, 11, 824-832
    • (1975) Mol. Pharmacol. , vol.11 , pp. 824-832
    • Sudlow, G.1    Birkett, D.J.2    Wade, D.N.3
  • 49
    • 0017763544 scopus 로고
    • Effects of fatty acids on two specific drug binding sites on human serum albumin
    • Birkett, D. J.; Myers, S. P.; Sudlow, G. Effects of fatty acids on two specific drug binding sites on human serum albumin Mol. Pharmacol. 1977, 13, 987-992
    • (1977) Mol. Pharmacol. , vol.13 , pp. 987-992
    • Birkett, D.J.1    Myers, S.P.2    Sudlow, G.3
  • 50
    • 0017382011 scopus 로고
    • Independent binding of ligands to human serum albumin
    • Brodersen, R.; Sjödin, T.; Sjöholm, I. Independent binding of ligands to human serum albumin J. Biol. Chem. 1977, 252, 5067-5072
    • (1977) J. Biol. Chem. , vol.252 , pp. 5067-5072
    • Brodersen, R.1    Sjödin, T.2    Sjöholm, I.3
  • 51
    • 0000123455 scopus 로고
    • Fluorometric determination of drug-protein association constants: The binding of 8-anilino-1-naphthalenesulfonate by bovine serum albumin
    • Naik, D. V.; Paul, W. L.; Threatte, R. M.; Schulman, S. G. Fluorometric determination of drug-protein association constants: The binding of 8-anilino-1-naphthalenesulfonate by bovine serum albumin Anal. Chem. 1975, 47, 267-270
    • (1975) Anal. Chem. , vol.47 , pp. 267-270
    • Naik, D.V.1    Paul, W.L.2    Threatte, R.M.3    Schulman, S.G.4
  • 52
    • 0013800421 scopus 로고
    • The interaction of a naphthalene dye with apomyoglobin and apohemoglobin: A fluorescent probe of non-polar binding sites
    • Stryer, L. The interaction of a naphthalene dye with apomyoglobin and apohemoglobin: A fluorescent probe of non-polar binding sites J. Mol. Biol. 1965, 13, 482-495
    • (1965) J. Mol. Biol. , vol.13 , pp. 482-495
    • Stryer, L.1
  • 53
    • 40549127817 scopus 로고    scopus 로고
    • A fluorescence analysis of ANS bound to bovine serum albumin: Binding properties revisited by using energy transfer
    • Togashi, D. M.; Ryder, A. G. A fluorescence analysis of ANS bound to bovine serum albumin: Binding properties revisited by using energy transfer J. Fluoresc. 2008, 18, 519-526
    • (2008) J. Fluoresc. , vol.18 , pp. 519-526
    • Togashi, D.M.1    Ryder, A.G.2
  • 54
    • 83455206060 scopus 로고    scopus 로고
    • Interaction of gold nanoparticle with human serum albumin (HSA) protein using surface energy transfer
    • Sen, T.; Mandal, S.; Haldar, S.; Chattopadhyay, K.; Patra, A. Interaction of gold nanoparticle with human serum albumin (HSA) protein using surface energy transfer J. Phys. Chem. C 2011, 115, 24037-24044
    • (2011) J. Phys. Chem. C , vol.115 , pp. 24037-24044
    • Sen, T.1    Mandal, S.2    Haldar, S.3    Chattopadhyay, K.4    Patra, A.5
  • 56
    • 0028959773 scopus 로고
    • Circular dichroism
    • Woody, R. W. Circular dichroism Methods Enzymol. 1995, 246, 34-71
    • (1995) Methods Enzymol. , vol.246 , pp. 34-71
    • Woody, R.W.1
  • 57
    • 84859524651 scopus 로고    scopus 로고
    • Spectral characterization of the binding and conformational changes of serum albumins upon interaction with an anticancer drug, anastrozole
    • Punith, R.; Seetharamappa, J. Spectral characterization of the binding and conformational changes of serum albumins upon interaction with an anticancer drug, anastrozole Spectrochim. Acta, Part A 2012, 92, 37-41
    • (2012) Spectrochim. Acta, Part A , vol.92 , pp. 37-41
    • Punith, R.1    Seetharamappa, J.2
  • 58
    • 34547684751 scopus 로고
    • Partly quenched, synchronously excited fluorescence emission spectra in the characterisation of complex mixtures
    • Lloyd, J. B. F. Partly quenched, synchronously excited fluorescence emission spectra in the characterisation of complex mixtures Analyst 1974, 99, 729-738
    • (1974) Analyst , vol.99 , pp. 729-738
    • Lloyd, J.B.F.1
  • 60
    • 84858678912 scopus 로고    scopus 로고
    • Affinity of two novel five-coordinated anticancer Pt(II) complexes to human and bovine serum albumins: A spectroscopic approach
    • Samari, F.; Hemmateenejad, B.; Shamsipur, M.; Rashidi, M.; Samouei, H. Affinity of two novel five-coordinated anticancer Pt(II) complexes to human and bovine serum albumins: A spectroscopic approach Inorg. Chem. 2012, 51, 3454-3464
    • (2012) Inorg. Chem. , vol.51 , pp. 3454-3464
    • Samari, F.1    Hemmateenejad, B.2    Shamsipur, M.3    Rashidi, M.4    Samouei, H.5
  • 61
    • 83655184700 scopus 로고    scopus 로고
    • Exploring the binding mechanism of ondansetron hydrochloride to serum albumins: Spectroscopic approach
    • Sandhya, B.; Hegde, A. H.; Ramesh, K. C.; Seetharamappa, J. Exploring the binding mechanism of ondansetron hydrochloride to serum albumins: Spectroscopic approach Spectrochim. Acta, Part A 2012, 86, 410-416
    • (2012) Spectrochim. Acta, Part A , vol.86 , pp. 410-416
    • Sandhya, B.1    Hegde, A.H.2    Ramesh, K.C.3    Seetharamappa, J.4
  • 62
    • 79952758069 scopus 로고    scopus 로고
    • Determination of triterpenic acids in human serum by high-performance liquid chromatography: Triterpenoid interaction with serum protein
    • Rada, M.; Ruiz-Gutiérrez, V.; Guinda, A. Determination of triterpenic acids in human serum by high-performance liquid chromatography: Triterpenoid interaction with serum protein J. Agric. Food Chem. 2011, 59, 2308-2313
    • (2011) J. Agric. Food Chem. , vol.59 , pp. 2308-2313
    • Rada, M.1    Ruiz-Gutiérrez, V.2    Guinda, A.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.