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Volumn 8, Issue 2, 1998, Pages 83-86

What may be bovine β-lactoglobulin Cys121 good for?

Author keywords

Baric oligomerisation; Chemical modification; High sensitivity differential scanning calorimetry; Lactoglobulin; Stability

Indexed keywords

ALPHA LACTALBUMIN; BETA LACTOGLOBULIN; CATTLE; DENATURATION; DIFFERENTIAL SCANNING CALORIMETRY; DISULFIDE; GEL PERMEATION CHROMATOGRAPHY; HIGH PERFORMANCE LIQUID CHROMATOGRAPHY; PH;

EID: 0032003976     PISSN: 09586946     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0958-6946(98)00023-5     Document Type: Article
Times cited : (9)

References (10)
  • 1
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    • Cunningham, L.W.1    Nuenke, B.J.2
  • 2
    • 0000419870 scopus 로고
    • Analysis of modified β-lactoglobulins and ovalbumins prepared from sulfenyl iodide intermediates
    • Cunningham, L. W. and Nuenke, B. J. (1960) Analysis of modified β-lactoglobulins and ovalbumins prepared from sulfenyl iodide intermediates. Journal of Biological Chemistry 235, 1711-1715.
    • (1960) Journal of Biological Chemistry , vol.235 , pp. 1711-1715
    • Cunningham, L.W.1    Nuenke, B.J.2
  • 3
    • 0000073862 scopus 로고
    • Mutational analysis of protein folding and stability
    • ed. T. E. Creighton. Freeman, New York
    • Goldenberg, D. P. (1992) Mutational analysis of protein folding and stability. In: Protein Folding, ed. T. E. Creighton. Freeman, New York.
    • (1992) Protein Folding
    • Goldenberg, D.P.1
  • 5
    • 84987300635 scopus 로고
    • Preparation of β-lactoglobulin and β-lactoglobulin-free proteins from whey retentate by NaCl salting our at low pH
    • Maillart, P. and Ribadeau-Dumas, B. (1988) Preparation of β-lactoglobulin and β-lactoglobulin-free proteins from whey retentate by NaCl salting our at low pH. Journal of Food Science 33, 743-752.
    • (1988) Journal of Food Science , vol.33 , pp. 743-752
    • Maillart, P.1    Ribadeau-Dumas, B.2
  • 6
    • 0015075957 scopus 로고
    • The denaturation of proteins: Two state? Reversible or irreversible?
    • McKenzie, H. A. and Ralston, G. B. (1971) The denaturation of proteins: two state? Reversible or irreversible? Experientia 27, 617-744.
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    • McKenzie, H.A.1    Ralston, G.B.2
  • 7
    • 0023661017 scopus 로고
    • Crystal structure of the trigonal form of bovine β-lactoglobulin and its complex with retinol at 2.5 Å resolution
    • Monaco, H. L., Zanotti, G., Spadon, P., Bolognesi, M., Sawyer, L. and Eliopoulos, E. E. (1987) Crystal structure of the trigonal form of bovine β-lactoglobulin and its complex with retinol at 2.5 Å resolution. Journal of Molecular Biology 197, 695-706.
    • (1987) Journal of Molecular Biology , vol.197 , pp. 695-706
    • Monaco, H.L.1    Zanotti, G.2    Spadon, P.3    Bolognesi, M.4    Sawyer, L.5    Eliopoulos, E.E.6
  • 8
    • 0018588511 scopus 로고
    • Stability of proteins: Small globular proteins
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    • (1979) Advances in Protein Chemistry , vol.33 , pp. 167-241
    • Privalov, P.L.1
  • 9
    • 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. and Seller, 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    Seller, P.4
  • 10
    • 0028095182 scopus 로고
    • Buried waters and internal cavities in monomeric proteins
    • Williams, M. A., Goodfellow, J. M. and Thornton, J. M. (1994) Buried waters and internal cavities in monomeric proteins. Protein Science 3, 1224-1235.
    • (1994) Protein Science , vol.3 , pp. 1224-1235
    • Williams, M.A.1    Goodfellow, J.M.2    Thornton, J.M.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.