Role of the intersubunit disulfide bond in the unfolding pathway of dimeric red kidney bean purple acid phosphatase.
作者： Anil G. Cashikar , N.Madhusudhana Rao
DOI: 10.1016/0167-4838(96)00055-6
关键词:
摘要: Quantitative equilibrium denaturation studies on oligomeric proteins have the potential to provide information role of subunit interactions in protein function and structure. We studied red kidney bean purple acid phosphatase (KBPAP), a homodimer with single disulfide bond between two subunits, an objective understand intersubunit KBPAP Binding 8-anilino-1-naphthalenesulfonic acid, enzymatic activity, size-exclusion chromatography, tryptophan fluorescence circular dichroism revealed that undergoes unfolding through at least three intermediates. Susceptibility for increases reduction aggregation was predominant product denaturation. In terms stability, contributes 25% overall stability dimer.
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