메뉴 건너뛰기




Volumn 78, Issue 4, 2002, Pages 443-455

Structural changes induced in bovine serum albumin by covalent attachment of chlorogenic acid

Author keywords

BSA; Chlorogenic acid; DSC; Food protein derivatization; Hydrophobicity; In vitro proteolytic degradation; Physicochemical characterization; Structure

Indexed keywords

8 ANILINO 1 NAPHTHALENESULFONIC ACID; BOVINE SERUM ALBUMIN; CHLOROGENIC ACID; CYSTEINE; LYSINE; TRYPTOPHAN;

EID: 0036768548     PISSN: 03088146     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0308-8146(02)00155-3     Document Type: Article
Times cited : (215)

References (27)
  • 1
    • 0018536145 scopus 로고
    • Determination of the degree of hydrolysis of food protein hydrolysates by trinitrobenzenesulfonic acid
    • Adler-Nissen J. Determination of the degree of hydrolysis of food protein hydrolysates by trinitrobenzenesulfonic acid. Journal of Agricultural & Food Chemistry. 27:1972;1256-1262.
    • (1972) Journal of Agricultural & Food Chemistry , vol.27 , pp. 1256-1262
    • Adler-Nissen, J.1
  • 2
    • 0030968136 scopus 로고    scopus 로고
    • Multiple interactions between polyphenols and a salivary proline-rich protein repeat result in complexation and precipitation
    • Baxter N.J., Lilley T.H., Haslam E., Williamson M.P. Multiple interactions between polyphenols and a salivary proline-rich protein repeat result in complexation and precipitation. Biochemistry. 36:1997;5566-5577.
    • (1997) Biochemistry , vol.36 , pp. 5566-5577
    • Baxter, N.J.1    Lilley, T.H.2    Haslam, E.3    Williamson, M.P.4
  • 3
    • 0003155058 scopus 로고
    • Commercially available proteases
    • R.J. Beynon, & J.S. Bond. Oxford: IRL Press
    • Bond J.S. Commercially available proteases. Beynon R.J., Bond J.S. Proteolytic enzymes. 1989;232-240 IRL Press, Oxford.
    • (1989) Proteolytic enzymes , pp. 232-240
    • Bond, J.S.1
  • 4
    • 0033385320 scopus 로고    scopus 로고
    • Grafting of aliphatic and aromatic probes on rapeseed 2S and 12S proteins: Influence on their structural and physicochemical properties
    • Gerbanowski A., Malabat C., Rabiller C., Guéguen J. Grafting of aliphatic and aromatic probes on rapeseed 2S and 12S proteins. Influence on their structural and physicochemical properties Journal of Agricultural & Food Chemistry. 47:1999;5218-5226.
    • (1999) Journal of Agricultural & Food Chemistry , vol.47 , pp. 5218-5226
    • Gerbanowski, A.1    Malabat, C.2    Rabiller, C.3    Guéguen, J.4
  • 5
  • 6
    • 85004830091 scopus 로고
    • Stability of vicilin, a legume seed storage protein, with step-wise electrostatic modification
    • Ismond M.A.H., Murray E.D., Arntfield S.D. Stability of vicilin, a legume seed storage protein, with step-wise electrostatic modification. Int. J. Peptide Protein Res. 26:1985;584-590.
    • (1985) Int. J. Peptide Protein Res. , vol.26 , pp. 584-590
    • Ismond, M.A.H.1    Murray, E.D.2    Arntfield, S.D.3
  • 7
    • 0012976086 scopus 로고
    • The role of noncovalent forces in micelle formation by vicillin from Vicia faba. III. The effect of urea, Guanidine Hydrochloride and sucrose on protein interactions
    • Ismond M.A.H., Murray E.D., Arntfield S.D. The role of noncovalent forces in micelle formation by vicillin from Vicia faba. III. The effect of urea, Guanidine Hydrochloride and sucrose on protein interactions. Food Chemistry. 29:1988;189-198.
    • (1988) Food Chemistry , vol.29 , pp. 189-198
    • Ismond, M.A.H.1    Murray, E.D.2    Arntfield, S.D.3
  • 8
    • 0000887242 scopus 로고
    • Ultraviolet absorption and fluorescence properties of whey-potato and whey-pea protein composites
    • Jackman J.L., Yada R.Y. Ultraviolet absorption and fluorescence properties of whey-potato and whey-pea protein composites. Can. Inst. Food Sci. Technol. J. 22:1989;252-259.
    • (1989) Can. Inst. Food Sci. Technol. J. , vol.22 , pp. 252-259
    • Jackman, J.L.1    Yada, R.Y.2
  • 9
    • 0033562629 scopus 로고    scopus 로고
    • Analyzing protein circular dichroism spectra for accurate secondary structures
    • Johnson W.C. Jr. Analyzing protein circular dichroism spectra for accurate secondary structures. Proteins: Structure & Function Genetetics. 35:1999;307-312.
    • (1999) Proteins: Structure & Function Genetetics , vol.35 , pp. 307-312
    • Johnson W.C., Jr.1
  • 11
    • 0035079945 scopus 로고    scopus 로고
    • Reactions of plant phenols with myoglobin: Influence of chemical structure of the phenolic compounds
    • Kroll J., Rawel H. Reactions of plant phenols with myoglobin. Influence of chemical structure of the phenolic compounds Journal of Food Science. 66(1):2001;48-58.
    • (2001) Journal of Food Science , vol.66 , Issue.1 , pp. 48-58
    • Kroll, J.1    Rawel, H.2
  • 12
    • 0034069971 scopus 로고    scopus 로고
    • Physicochemical properties and susceptibility to proteolytic digestion of myoglobin-phenol derivatives
    • Kroll J., Rawel H., Seidelmann N. Physicochemical properties and susceptibility to proteolytic digestion of myoglobin-phenol derivatives. Journal of Agricultural & Food Chemistry. 48(5):2000;1580-1587.
    • (2000) Journal of Agricultural & Food Chemistry , vol.48 , Issue.5 , pp. 1580-1587
    • Kroll, J.1    Rawel, H.2    Seidelmann, N.3
  • 13
    • 0012983408 scopus 로고
    • Buried and exposed groups in proteins
    • G.D. Fasman, & S.N. Timasheff. New York, NY: Marcel Dekker
    • Kronman M.J., Robbins F.M. Buried and exposed groups in proteins. Fasman G.D., Timasheff S.N. Fine structure of proteins and nucleic acids. 1970;271 Marcel Dekker, New York, NY.
    • (1970) Fine structure of proteins and nucleic acids , pp. 271
    • Kronman, M.J.1    Robbins, F.M.2
  • 14
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T
    • Laemmli U.K. Cleavage of structural proteins during the assembly of the head of bacteriophage T. Nature. 277:1970;680-685.
    • (1970) Nature , vol.277 , pp. 680-685
    • Laemmli, U.K.1
  • 16
    • 0000476953 scopus 로고
    • The reaction of quinones with protamine and nucleoprotamine: N-terminal proline
    • Mason H.S., Peterson E.W. The reaction of quinones with protamine and nucleoprotamine. N-terminal proline Journal of Biological Chemistry. 212:1955;485-493.
    • (1955) Journal of Biological Chemistry , vol.212 , pp. 485-493
    • Mason, H.S.1    Peterson, E.W.2
  • 17
    • 0029032420 scopus 로고
    • Interaction of 3′-O-caffeoyl D-quinic acid with human serum albumin
    • Muralidhara B.K., Prakash V. Interaction of 3′-O-caffeoyl D-quinic acid with human serum albumin. Int. J. Peptide Protein Res. 46:1995;1-8.
    • (1995) Int. J. Peptide Protein Res. , vol.46 , pp. 1-8
    • Muralidhara, B.K.1    Prakash, V.2
  • 18
    • 0028143645 scopus 로고
    • Quantitative electrophoretic analysis of proteins labeled with monobrimane
    • O'Keefe D.O. Quantitative electrophoretic analysis of proteins labeled with monobrimane. Analytical Biochemistry. 222:1994;86-94.
    • (1994) Analytical Biochemistry , vol.222 , pp. 86-94
    • O'Keefe, D.O.1
  • 19
    • 0041524991 scopus 로고    scopus 로고
    • Model studies on reactions of plant phenols with whey proteins
    • Rawel H., Kroll J., Hohl U.C. Model studies on reactions of plant phenols with whey proteins. Nahrung/Food. 45(2):2001;72-81.
    • (2001) Nahrung/Food , vol.45 , Issue.2 , pp. 72-81
    • Rawel, H.1    Kroll, J.2    Hohl, U.C.3
  • 20
    • 0033768560 scopus 로고    scopus 로고
    • Reactions of chlorogenic acid with lysozyme- physicochemical characterisation and proteolytic digestion of the derivatives
    • Rawel H., Kroll J., Riese B. Reactions of chlorogenic acid with lysozyme- physicochemical characterisation and proteolytic digestion of the derivatives. Journal of Food Science. 65(6):2000;1091-1098.
    • (2000) Journal of Food Science , vol.65 , Issue.6 , pp. 1091-1098
    • Rawel, H.1    Kroll, J.2    Riese, B.3
  • 21
    • 0035238955 scopus 로고    scopus 로고
    • Reactions of phenolic substances with lysozyme-physicochemical characterisation and proteolytic digestion of the derivatives
    • Rawel H., Kroll J., Rohn S. Reactions of phenolic substances with lysozyme-physicochemical characterisation and proteolytic digestion of the derivatives. Food Chemistry. 72(1):2001;59-71.
    • (2001) Food Chemistry , vol.72 , Issue.1 , pp. 59-71
    • Rawel, H.1    Kroll, J.2    Rohn, S.3
  • 22
    • 0001541402 scopus 로고    scopus 로고
    • Reactions of selected secondary plant metabolites (glucosinolates and phenols) with food proteins and enzymes - influence on physico-chemical protein properties, enzyme activity and proteolytic degradation
    • India: Research Signpost
    • Rawel, H., Rohn, S., & Kroll, J. (2000). Reactions of selected secondary plant metabolites (glucosinolates and phenols) with food proteins and enzymes - influence on physico-chemical protein properties, enzyme activity and proteolytic degradation. In Recent research developments in phytochemistry, Vol. 4 (pp. 115-142). India: Research Signpost.
    • (2000) Recent Research Developments in Phytochemistry , vol.4 , pp. 115-142
    • Rawel, H.1    Rohn, S.2    Kroll, J.3
  • 24
    • 0032967327 scopus 로고    scopus 로고
    • Effects of protein-polyphenol interactions on beverage haze, stabilization, and analysis
    • Siebert K.J. Effects of protein-polyphenol interactions on beverage haze, stabilization, and analysis. Journal of Agricultural & Food Chemistry. 47:1999;353-362.
    • (1999) Journal of Agricultural & Food Chemistry , vol.47 , pp. 353-362
    • Siebert, K.J.1
  • 26
    • 0034672325 scopus 로고    scopus 로고
    • Estimation of protein secondary structure from circular dichroism spectra: Comparison of CONTIN, SELCON and CDSSTR methods with an expanded reference set
    • Sreerama N., Woody R.W. Estimation of protein secondary structure from circular dichroism spectra. comparison of CONTIN, SELCON and CDSSTR methods with an expanded reference set Analytical Biochemistry. 287:2000;252-260.
    • (2000) Analytical Biochemistry , vol.287 , pp. 252-260
    • Sreerama, N.1    Woody, R.W.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.