P-lactoglobulin, bovine

The ROA spectra of hen lysozyme [3, 35] and bovine P-lactoglobulin [3] are shown in Fig. 7.5. These spectra contain marker bands for the secondary structural motifs discussed above showing that this information is retained... [Pg.160]

Miller, K., Meredith, C., Selo, I., and Wal, J.M. 1999. Allergy to bovine P-lactoglobulin Specificity of immunoglobulin E generated in the brown Norway rat to tryptic and synthetic peptides. Clin Exp Allergy 29 1696-1704. [Pg.200]

FIGURE 35.1 Structure of fi-LG with p strands and joining loops labeled. (Reprinted from Structure, 5(1), Brownlow, S., Morais, C.J.H., Cooper, R., Hower, D.R., Yewdall, S.J., Polikarpov, I., North, A.C.T., and Sawyer, L., Bovine p-lactoglobulin at 1.8 A resolution-still an enigmatic lipocalin, 481-495. Copyright 1997, with permission from Elsevier.)... [Pg.730]

Kontopidis, G. Holt, C. Sawyer, L. The ligand-binding site of bovine P-lactoglobulin Evidence for a function J. Mol. Biol. 2002,318 (4), 1043-1055. [Pg.737]

Sakurai, K. Goto, Y. Dynamics and mechanism of the tanford transition of bovine P-lactoglobulin studied using heteronuclear NMR spectroscopy. J. Mol. Biol. 2006, 356 (2), 483—496. [Pg.737]

Sakurai, K. Goto, Y. Principal component analysis of the pH-dependent conformational transitions of bovine p-lactoglobulin monitored by heteronuclear NMR. PNAS 2007,104 (39), 15346-15351. [Pg.737]

Mousavi, S.H. Bordbar, A.K. Haertle, T. Changes in structure and in interactions of heat-treated bovine P-lactoglobulin. Protein Pept. Lett. 2008,15 (8), 818-825. [Pg.737]

Ruyol, R Rtrez, M.D. Reiro, J.M. Calvo, M. Effect of retinol and fatty acid binding to bovine P-lactoglobulin on its resistance to thermal denaturation. J. Dairy Sci. 1994, 77 (6), 1494. [Pg.738]

Creamer, L.K. Effect of sodium dodecyl sulfate and palmitic acid on the equilibrium unfolding of bovine P-lactoglobulin. Biochemistry 1995,34 (21), 7170-7176. [Pg.738]

Lange, D.C. Kothari, R. Patel, R.C. Patel, S.C. Retinol and retinoic acid bind to a surface cleft in bovine P-lactoglobulin A method of binding site determination using fluorescence resonance energy transfer. Biophys. Chem. 1998, 74 (1), 45-51. [Pg.738]

Shimoyamada, M. Yoshimura, H. Tomida, K. Watanabe, K. Stabilities of bovine P-lactoglobulin/reti-nol or retinoic acid complexes against tryptic hydrolysis, heating and light-induced oxidation. Lebensm. Wiss. u. Technol. 1996, 29 (8), 763-766. [Pg.738]

Barbiroli, A. Bonomi, R Ferranti, P. Fessas, D. Nasi, A. Rasmussen, P Lametti, S. Bound fatty acids modulate the sensitivity of bovine P-Lactoglobulin to chemical and physical denaturation. J. Agric. Food Chem. 2011, 59 (10), 5729-5737. [Pg.739]

Collini, M. D Alfonso, L. Molinari, H. Ragona, L. Catalano, M. Baldini, G. Competitive binding of fatty acids and the fluorescent probe 1-8-anilinonaphthalene sulfonate to bovine P-lactoglobulin. Protein Sci. 2003,12 (8), 1596-1603. [Pg.739]

Brownlow S, Cabral JHM, Cooper R et al (1997) Bovine p-lactoglobulin at 1.8 Angstrom resolution - still an enigmatic lipocalin. Structure 5(4) 481-495... [Pg.96]

Sawyer L, Kontopidis G (2000) The core lipocalin, bovine p-lactoglobulin. Biochem Biophys Acta 1482 136-148... [Pg.96]

Hattori, M. Ametani, A. Katakura, Y Shimizu, M. Kaminogawa, S. Unfolding/refolding studies on bovine p-lactoglobulin with monoclonal antibodies as probes. Does a renatured protein completely refold J. Biol. Chem. 1993, 268, 22414-22419. [Pg.22]

F. Fogolari, L. Ragona, S. Licciardi, S. Romagnoli, R. Michelutti, R. Ugolini, and H. Molinari, Proteins Struct. Funct. Genet., 39, 317 (2000). Electrostatic Properties of Bovine P-Lactoglobulin. [Pg.358]

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