메뉴 건너뛰기




Volumn 54, Issue 1, 1997, Pages 40-49

Preliminary characterization of bovine beta-lactoglobulin after its conjugation to polyethylene glycol

Author keywords

conformation; immunogenicity; pegylation; plasma clearance; retinol binding; whey proteins

Indexed keywords

ACYLATION; AMINO ACIDS; BIOTECHNOLOGY; CONFORMATIONS; FOURIER TRANSFORM INFRARED SPECTROSCOPY; GRAFTING (CHEMICAL); IMMUNOLOGY; MOLECULAR STRUCTURE; PHARMACODYNAMICS; POLYETHYLENE GLYCOLS;

EID: 0031553986     PISSN: 00063592     EISSN: None     Source Type: Journal    
DOI: 10.1002/(SICI)1097-0290(19970405)54:1<40::AID-BIT5>3.0.CO;2-Y     Document Type: Article
Times cited : (15)

References (33)
  • 1
    • 0028241249 scopus 로고
    • Model for predicting the partition behaviour of proteins in aqueous two-phase systems
    • Asenjo, J. A., Schmidt, A. S., Hachem, F., Andrews, B. A. 1994. Model for predicting the partition behaviour of proteins in aqueous two-phase systems. J. Chromatogr. 668: 47-54.
    • (1994) J. Chromatogr. , vol.668 , pp. 47-54
    • Asenjo, J.A.1    Schmidt, A.S.2    Hachem, F.3    Andrews, B.A.4
  • 2
    • 0030022922 scopus 로고
    • S-pegylthiopapain, a versatile intermediate for the preparation of the fully active form of the cysteine proteinase archetype
    • Azarkan, M., Wintjens, R. T., Smolders, N., Nijs, M., Looze, Y. 1995. S-pegylthiopapain, a versatile intermediate for the preparation of the fully active form of the cysteine proteinase archetype. J. Chromatogr. 724: 185-192.
    • (1995) J. Chromatogr. , vol.724 , pp. 185-192
    • Azarkan, M.1    Wintjens, R.T.2    Smolders, N.3    Nijs, M.4    Looze, Y.5
  • 4
    • 51249181265 scopus 로고
    • Complex formation in sonicated mixtures of β-lactoglobulin and phosphatidycholine
    • Brown, E. M., Carroll, R. J., Pfeffer, P. E., Sampugna, J. 1983. Complex formation in sonicated mixtures of β-lactoglobulin and phosphatidycholine. Lipids 18: 111-118.
    • (1983) Lipids , vol.18 , pp. 111-118
    • Brown, E.M.1    Carroll, R.J.2    Pfeffer, P.E.3    Sampugna, J.4
  • 5
    • 0023802035 scopus 로고
    • Accessibility and mobility of lysine residues in β-lactoglobulin
    • Brown, E. M., Pfeffer, P. E., Kumosinski, T. F., Greenberg, R. 1988. Accessibility and mobility of lysine residues in β-lactoglobulin. Biochemistry 27: 5601-5610.
    • (1988) Biochemistry , vol.27 , pp. 5601-5610
    • Brown, E.M.1    Pfeffer, P.E.2    Kumosinski, T.F.3    Greenberg, R.4
  • 6
    • 0023693897 scopus 로고
    • Structural and conformational changes of β-lactoglobulin B: An infrared spectroscopic study of the effect of pH and temperature
    • Casal, H. L., Köhler, U., Manisch, H. H. 1988. Structural and conformational changes of β-lactoglobulin B: an infrared spectroscopic study of the effect of pH and temperature. Biochim. Biophys. Acta 957: 11-20.
    • (1988) Biochim. Biophys. Acta , vol.957 , pp. 11-20
    • Casal, H.L.1    Köhler, U.2    Manisch, H.H.3
  • 7
    • 0026659050 scopus 로고
    • IgG antibody response to polyethylene glycol-modified adenosine deaminase in patients with adenosine deaminase deficiency
    • Chaffee, S., Mary, A., Stiehm, E. R., Girault, D., Fischer, A., Hershfield, M. S. 1992. IgG antibody response to polyethylene glycol-modified adenosine deaminase in patients with adenosine deaminase deficiency. J. Clin. Invest. 89: 1643-1651.
    • (1992) J. Clin. Invest. , vol.89 , pp. 1643-1651
    • Chaffee, S.1    Mary, A.2    Stiehm, E.R.3    Girault, D.4    Fischer, A.5    Hershfield, M.S.6
  • 8
    • 0028246854 scopus 로고
    • Probing the retinol-binding site of bovine β-lactoglobulin
    • Cho, Y., Batt, C. A., Sawyer, L. 1994. Probing the retinol-binding site of bovine β-lactoglobulin. J. Biol. Chem. 269: 11102-11107.
    • (1994) J. Biol. Chem. , vol.269 , pp. 11102-11107
    • Cho, Y.1    Batt, C.A.2    Sawyer, L.3
  • 9
    • 0028965716 scopus 로고
    • Impact of esterification on the folding and the susceptibility to peptic proteolysis of beta-lactoglobulin
    • Chobert, J. M., Briand, L., Grinberg, V., Haertlé, T. 1995. Impact of esterification on the folding and the susceptibility to peptic proteolysis of beta-lactoglobulin. Biochim. Biophys. Acta 1248: 170-176.
    • (1995) Biochim. Biophys. Acta , vol.1248 , pp. 170-176
    • Chobert, J.M.1    Briand, L.2    Grinberg, V.3    Haertlé, T.4
  • 10
    • 0025155418 scopus 로고
    • Binding of ellipticine to β-lactoglobulin: A physico-chemical study of the specific interaction of an antitumor drug with a transport protein
    • Dodin, G., Andrieux, M., Al Kabbani, H. 1990. Binding of ellipticine to β-lactoglobulin: A physico-chemical study of the specific interaction of an antitumor drug with a transport protein. Eur. J. Biochem. 193: 697-700.
    • (1990) Eur. J. Biochem. , vol.193 , pp. 697-700
    • Dodin, G.1    Andrieux, M.2    Al Kabbani, H.3
  • 11
    • 0028916150 scopus 로고
    • Infrared spectroscopic studies of lyophilization and temperature induced protein aggregation
    • Dong, A. C. Prestreilski, S. J., Allison, S. D., Carpenter, J. F. 1995. Infrared spectroscopic studies of lyophilization and temperature induced protein aggregation. J. Pharm. Sci. 84: 415-424.
    • (1995) J. Pharm. Sci. , vol.84 , pp. 415-424
    • Dong, A.C.1    Prestreilski, S.J.2    Allison, S.D.3    Carpenter, J.F.4
  • 12
    • 0001510699 scopus 로고
    • Binding affinities of β-ionone and related flavor compounds to β-lactoglobulin: Effect of chemical modifications
    • Dufour, E., Haertlé, T. 1990. Binding affinities of β-ionone and related flavor compounds to β-lactoglobulin: Effect of chemical modifications. J. Agric. Food Chem. 38: 1691-1695.
    • (1990) J. Agric. Food Chem. , vol.38 , pp. 1691-1695
    • Dufour, E.1    Haertlé, T.2
  • 13
    • 0025784171 scopus 로고
    • Binding of retinoids and β-carotene to β-lactoglobulin. Influence of protein modifications
    • Dufour, E., Haertlé, T. 1991. Binding of retinoids and β-carotene to β-lactoglobulin. Influence of protein modifications. Biochim. Biophys. Acta 1079: 316-320.
    • (1991) Biochim. Biophys. Acta , vol.1079 , pp. 316-320
    • Dufour, E.1    Haertlé, T.2
  • 14
    • 0026615889 scopus 로고
    • Binding of benzo(a)pyrene, ellipticine, and cis-parinaric acid to beta-lactoglobulin: Influence of protein modifications
    • Dufour, E., Roger, P., Haertlé, T. 1992. Binding of benzo(a)pyrene, ellipticine, and cis-parinaric acid to beta-lactoglobulin: Influence of protein modifications. J. Protein Chem. 11: 645-652.
    • (1992) J. Protein Chem. , vol.11 , pp. 645-652
    • Dufour, E.1    Roger, P.2    Haertlé, T.3
  • 15
    • 0027578704 scopus 로고
    • Reversible effects of medium dielectric constant on structural transformation of beta-lactoglobulin and its retinol binding
    • Dufour, E., Harb, C., Haertlé, T. 1993. Reversible effects of medium dielectric constant on structural transformation of beta-lactoglobulin and its retinol binding. Biopolymers 33: 589-598.
    • (1993) Biopolymers , vol.33 , pp. 589-598
    • Dufour, E.1    Harb, C.2    Haertlé, T.3
  • 16
    • 0027522088 scopus 로고
    • Probing the fatty acid binding site for β-lactoglobulins
    • Frapin, D., Dufour, E., Haertlé, T. 1993. Probing the fatty acid binding site for β-lactoglobulins. J. Protein Chem. 12: 443-449.
    • (1993) J. Protein Chem. , vol.12 , pp. 443-449
    • Frapin, D.1    Dufour, E.2    Haertlé, T.3
  • 17
    • 0027263367 scopus 로고
    • Lipocalins: Do we taste with our tears?
    • Gachon, A. M. 1993. Lipocalins: Do we taste with our tears? (Letter) Trends Biochem. Sci. 18: 206-207.
    • (1993) Trends Biochem. Sci. , vol.18 , pp. 206-207
    • Gachon, A.M.1
  • 18
    • 0024448151 scopus 로고
    • Calculation of protein extinction coefficients from amino acid sequence data
    • Gill, S. C., von Hippel, P. H. 1989. Calculation of protein extinction coefficients from amino acid sequence data. Anal. Biochem. 182: 319-326.
    • (1989) Anal. Biochem. , vol.182 , pp. 319-326
    • Gill, S.C.1    Von Hippel, P.H.2
  • 19
    • 0023126491 scopus 로고
    • Study of the adriamycin-cardiolipin complex structure using attenuated total reflection infrared spectroscopy
    • Goormaghtigh, E., Brasseur, R., Huart, P., Ruysschaert, J. M. 1987. Study of the adriamycin-cardiolipin complex structure using attenuated total reflection infrared spectroscopy. Biochemistry 26: 1789-1794.
    • (1987) Biochemistry , vol.26 , pp. 1789-1794
    • Goormaghtigh, E.1    Brasseur, R.2    Huart, P.3    Ruysschaert, J.M.4
  • 20
    • 1842325211 scopus 로고
    • Test par capture de l'anticorps-détection et quantification des antigènes par compétition antigénique
    • E. Harlow and D. Lane (eds.), Pradel publ., Paris
    • Harlow, E., Lane, D. 1991. Test par capture de l'anticorps-détection et quantification des antigènes par compétition antigénique. pp. 570-573 In: E. Harlow and D. Lane (eds.), Anticorps: un manuel de laboratoire. Pradel publ., Paris.
    • (1991) Anticorps: Un Manuel de Laboratoire , pp. 570-573
    • Harlow, E.1    Lane, D.2
  • 21
    • 0027253357 scopus 로고
    • The conjugation of proteins with polyethylene glycol and other polymers. Altering properties of proteins to enhance their therapeutic potential
    • Katre, N. V. 1993. The conjugation of proteins with polyethylene glycol and other polymers. Altering properties of proteins to enhance their therapeutic potential. Adv. Drug Deliv. Rev. 10:91-114.
    • (1993) Adv. Drug Deliv. Rev. , vol.10 , pp. 91-114
    • Katre, N.V.1
  • 22
    • 0029018811 scopus 로고
    • Selective inhibition of bitter taste of various drugs lipoprotein
    • Katsuragi, Y., Sugiura, Y., Lee, C., Otsuji, K., Kurihara, K. 1995. Selective inhibition of bitter taste of various drugs lipoprotein. Pharm. Res. 12: 658-662.
    • (1995) Pharm. Res. , vol.12 , pp. 658-662
    • Katsuragi, Y.1    Sugiura, Y.2    Lee, C.3    Otsuji, K.4    Kurihara, K.5
  • 23
    • 0014969174 scopus 로고
    • The whey proteins of pig's milk. Isolation and characterization of a β-lactoglobulin
    • Kessler, E., Brew, K. 1970. The whey proteins of pig's milk. Isolation and characterization of a β-lactoglobulin. Biochim. Biophys. Acta 200: 449-458.
    • (1970) Biochim. Biophys. Acta , vol.200 , pp. 449-458
    • Kessler, E.1    Brew, K.2
  • 24
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli, U. K. 1970. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 227: 680-685.
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 25
    • 0021647713 scopus 로고
    • Wide-pore silica-based ether-bonded phases for separation and size-exclusion chromatography
    • Miller, N. T., Feibush, B., Karger, B. L. 1985. Wide-pore silica-based ether-bonded phases for separation and size-exclusion chromatography. J. Chromatogr. 316: 519-536.
    • (1985) J. Chromatogr. , vol.316 , pp. 519-536
    • Miller, N.T.1    Feibush, B.2    Karger, B.L.3
  • 26
    • 0023661017 scopus 로고
    • Crystal structure of the trigonal form of bovine beta-lactoglobulin and of its complex with retinol at 2.5 Å resolution
    • Monaco, H. L., Zonatti, G., Spadon, P. 1987. Crystal structure of the trigonal form of bovine beta-lactoglobulin and of its complex with retinol at 2.5 Å resolution. J. Mol. Biol. 197: 695-706.
    • (1987) J. Mol. Biol. , vol.197 , pp. 695-706
    • Monaco, H.L.1    Zonatti, G.2    Spadon, P.3
  • 29
    • 0026595106 scopus 로고
    • Effect of beta-lactoglobulin on the activity of pregastric lipase. A possible role for this protein in ruminant milk
    • Perez, M. D., Sanchez, L., Aranda, P., Ena, J. M., Oria, R., Calvo, M. 1992. Effect of beta-lactoglobulin on the activity of pregastric lipase. A possible role for this protein in ruminant milk. Biochim. Biophys. Acta 1123: 151-155.
    • (1992) Biochim. Biophys. Acta , vol.1123 , pp. 151-155
    • Perez, M.D.1    Sanchez, L.2    Aranda, P.3    Ena, J.M.4    Oria, R.5    Calvo, M.6
  • 30
    • 0028989763 scopus 로고
    • Uptake and passage of beta-lactoglobulin, palmitic acid and retinol across the caco-2 monolayer
    • Puyol, P., Perez, M. D., Sanchez, L., Ena, J. M., Calvo, M. 1995. Uptake and passage of beta-lactoglobulin, palmitic acid and retinol across the caco-2 monolayer. Biochim. Biophys. Acta 1236: 149-154.
    • (1995) Biochim. Biophys. Acta , vol.1236 , pp. 149-154
    • Puyol, P.1    Perez, M.D.2    Sanchez, L.3    Ena, J.M.4    Calvo, M.5
  • 31
    • 0028985708 scopus 로고
    • Thermal denaturation of beta-lactoglobulin. Effect of protein concentration at pH 6.75 and 8.05
    • Qi, X. L., Browniow, S., Holt, C., Sellers, P. 1995. Thermal denaturation of beta-lactoglobulin. Effect of protein concentration at pH 6.75 and 8.05. Biochim. Biophys. Acta 1248: 43-49.
    • (1995) Biochim. Biophys. Acta , vol.1248 , pp. 43-49
    • Qi, X.L.1    Browniow, S.2    Holt, C.3    Sellers, P.4
  • 32
    • 0022704801 scopus 로고
    • A fluorimetric assay of the degree of modification of protein primary amines with polyethylene glycol
    • Stocks, S. J., Jones, A. J. M., Romey, C. W., Brooks, D. E. 1986. A fluorimetric assay of the degree of modification of protein primary amines with polyethylene glycol. Anal. Biochem. 154: 232-234.
    • (1986) Anal. Biochem. , vol.154 , pp. 232-234
    • Stocks, S.J.1    Jones, A.J.M.2    Romey, C.W.3    Brooks, D.E.4
  • 33
    • 0027420461 scopus 로고
    • Localisation of T-cell determinants on bovine beta-lactoglobulin
    • Tsuji, N. M., Kurisaki, J., Mizumachi, K., Kaminogawa, S. 1993. Localisation of T-cell determinants on bovine beta-lactoglobulin. Immunol. Lett. 37: 215-221. ing the lyoprotectants. ©1997 John Wiley & Sons, Inc. Bio-technol Bioeng 54: 50-57, 1997.
    • (1993) Immunol. Lett. , vol.37 , pp. 215-221
    • Tsuji, N.M.1    Kurisaki, J.2    Mizumachi, K.3    Kaminogawa, S.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.