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Hydrophobic Probe Binding Of Β-Lactoglobulin In The Native And Molten Globule State Induced By High Pressure As Affected By Ph, Kio3 And N-Ethylmaleimide, Jian Yang, Joseph R. Powers, Stephanie Clark, A. Keith Dunker, Barry G. Swanson
Hydrophobic Probe Binding Of Β-Lactoglobulin In The Native And Molten Globule State Induced By High Pressure As Affected By Ph, Kio3 And N-Ethylmaleimide, Jian Yang, Joseph R. Powers, Stephanie Clark, A. Keith Dunker, Barry G. Swanson
Stephanie Clark
High hydrostatic pressure (HHP) at 500 MPa and 50 °C induces β-LG into the molten globule state. Retinol, cis-parinaric acid (CPA), and 1-anilino-naphthalene-8-sulfonate (ANS) fluorescence from pH 2.5 to 10.5 in the presence of the native and molten globule states of β-LG indicate that retinol binds to β-LG in the calyx, CPA at the surface hydrophobic site, and ANS in multiple hydrophobic sites. HHP treatment results in a decrease of β-LG affinity for retinol and CPA, suggesting conformational changes in the calyx and surface hydrophobic site of β-LG during HHP treatment. β-LG treated by HHP in the presence of N-ethylmaleimide …