메뉴 건너뛰기




Volumn 34, Issue 5-6, 1999, Pages 477-481

Effect of anions on the denaturation and aggregation of β-lactoglobulin as measured by differential scanning microcalorimetry

Author keywords

Microcalorimetry; Phosphate; Thermal stability; Lactoglobulin

Indexed keywords


EID: 0039374811     PISSN: 09505423     EISSN: None     Source Type: Journal    
DOI: 10.1046/j.1365-2621.1999.00316.x     Document Type: Article
Times cited : (21)

References (15)
  • 1
    • 0027942765 scopus 로고
    • Importance of the region around lysine-196 for catalytic activity of adenylyl-cyclase from Escherichia-coli
    • Amin, N. & Peterkofsky, A. (1994). Importance of the region around lysine-196 for catalytic activity of adenylyl-cyclase from Escherichia-Coli. Journal of Biological Chemistry, 269, 31074-31079.
    • (1994) Journal of Biological Chemistry , vol.269 , pp. 31074-31079
    • Amin, N.1    Peterkofsky, A.2
  • 2
    • 0032001691 scopus 로고    scopus 로고
    • Detection of intermediate oligomers, important for the formation of heat aggregates of β-lactoglobulin
    • Bauer, R., Hansen, S. & Øgendal, L. (1998). Detection of intermediate oligomers, important for the formation of heat aggregates of β-lactoglobulin. International Dairy Journal, 8, 105-112.
    • (1998) International Dairy Journal , vol.8 , pp. 105-112
    • Bauer, R.1    Hansen, S.2    ØGendal, L.3
  • 5
    • 0028987857 scopus 로고
    • Site-directed mutagenesis of P-2U purinoceptors-positively charged amino-acids in transmembrane helix-6 and helix-7 affect agonist potency and specificity
    • Erb, L., Garrad, R., Wang, Y.J., Quinn, T., Turner, J.T. & Weisman, G.A. (1995). Site-directed mutagenesis of P-2U purinoceptors-positively charged amino-acids in transmembrane helix-6 and helix-7 affect agonist potency and specificity. Journal of Biological Chemistry, 270, 4185-4188.
    • (1995) Journal of Biological Chemistry , vol.270 , pp. 4185-4188
    • Erb, L.1    Garrad, R.2    Wang, Y.J.3    Quinn, T.4    Turner, J.T.5    Weisman, G.A.6
  • 6
    • 0029945220 scopus 로고    scopus 로고
    • X-ray structure of yeast inorganic pyrophosphatase complexed with manganese and phosphate
    • Harutyunyan, E.H., Kuranova, I.P., Vainshtein, et al. (1996). X-ray structure of yeast inorganic pyrophosphatase complexed with manganese and phosphate. European Journal of Biochemistry, 239, 220-228.
    • (1996) European Journal of Biochemistry , vol.239 , pp. 220-228
    • Harutyunyan, E.H.1    Kuranova, I.P.2    Vainshtein3
  • 8
    • 0031999030 scopus 로고    scopus 로고
    • Comparison of the effect of heating on the thermal denaturation of nine different β-lactoglobulin presss of genetic variants A, B or A/B, as measured by microcalorimetry
    • Holt, C., Waninge, R., Sellers, P. et al. (1998). Comparison of the effect of heating on the thermal denaturation of nine different β-lactoglobulin presss of genetic variants A, B or A/B, as measured by microcalorimetry. International Dairy Journal, 8, 99-104.
    • (1998) International Dairy Journal , vol.8 , pp. 99-104
    • Holt, C.1    Waninge, R.2    Sellers, P.3
  • 9
    • 2142720593 scopus 로고    scopus 로고
    • Ion binding and ion specificity: The Hofmeister effect, Onsager and Lifshitz theories
    • Ninham, B.W. & Yaminsky, V. (1997). Ion binding and ion specificity: the Hofmeister effect, Onsager and Lifshitz theories. Langmuir, 13, 2097-2108.
    • (1997) Langmuir , vol.13 , pp. 2097-2108
    • Ninham, B.W.1    Yaminsky, V.2
  • 10
    • 0001253172 scopus 로고
    • Thermal-stability of whey proteins studied by differential scanning calorimetry
    • Paulsson, M., Hegg, P.-O. & Castberg, H.B. (1985). Thermal-stability of whey proteins studied by differential scanning calorimetry. Thermochim. Acta, 95, 435-440.
    • (1985) Thermochim. Acta , vol.95 , pp. 435-440
    • Paulsson, M.1    Hegg, P.-O.2    Castberg, H.B.3
  • 11
    • 0028985708 scopus 로고
    • Thermal denaturation of β-lactoglobulin: Effect of protein concentration at pH 6.75 and 8.05
    • Qi, X.L., Brownlow, S., Holt, C. & Sellers, P. (1995). Thermal denaturation of β-lactoglobulin: effect of protein concentration at pH 6.75 and 8.05. Biochimica et Biophysica Acta. 1248, 43-49.
    • (1995) Biochimica et Biophysica Acta. , vol.1248 , pp. 43-49
    • Qi, X.L.1    Brownlow, S.2    Holt, C.3    Sellers, P.4
  • 12
    • 0030993642 scopus 로고    scopus 로고
    • Effect of temperature on the secondary structure of β-lactoglobulin at pH 6.7, as determined by CD and IR spectroscopy: A test of the molten globule hypothesis
    • Qi, X.L., Holt, C., McNulty, D., Clarke, D.T., Brownlow, S. & Jones, G.R. (1997). Effect of temperature on the secondary structure of β-lactoglobulin at pH 6.7, as determined by CD and IR spectroscopy: a test of the molten globule hypothesis. Biochemistry Journal, 324, 341-346.
    • (1997) Biochemistry Journal , vol.324 , pp. 341-346
    • Qi, X.L.1    Holt, C.2    McNulty, D.3    Clarke, D.T.4    Brownlow, S.5    Jones, G.R.6
  • 13
    • 0039954967 scopus 로고
    • Study of heat denaturation of human serum-albumin in aqueous alcohol and aqueous salt-solutions in the presence of organic-ligands
    • Stepuro, I.I., Lapshina, E.A. & Chaikovskaya, N.A. (1991). Study of heat denaturation of human serum-albumin in aqueous alcohol and aqueous salt-solutions in the presence of organic-ligands. Molecular Biology, 25, 275-284.
    • (1991) Molecular Biology , vol.25 , pp. 275-284
    • Stepuro, I.I.1    Lapshina, E.A.2    Chaikovskaya, N.A.3
  • 14
    • 0039362684 scopus 로고
    • Electrostatic free energy and polyelectrolytes
    • New York: John Wiley
    • Tanford, C. (1966). Electrostatic free energy and polyelectrolytes. In: Physical Chemistry of Macromolecules. Pp. 457-525. New York: John Wiley.
    • (1966) Physical Chemistry of Macromolecules , pp. 457-525
    • Tanford, C.1
  • 15
    • 84971943452 scopus 로고
    • A differential scanning calonmetric study of the thermal behaviour of bovine β-lactoglobulin at temperatures up to 160 °C
    • de Wit, J. & Klarenbeek, G. (1981). A differential scanning calonmetric study of the thermal behaviour of bovine β-lactoglobulin at temperatures up to 160 °C. Journal of Dairy Research, 48, 293-302.
    • (1981) Journal of Dairy Research , vol.48 , pp. 293-302
    • De Wit, J.1    Klarenbeek, G.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.