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Interaction of Potassium Mono and Di Phosphates with Bovine Serum Albumin Studied by Fluorescence Quenching Method

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Abstract

The interactions between potassium mono and di phosphates and bovine serum albumin (BSA) were studied using fluorescence spectroscopy (FS) and ultraviolet spectroscopy (UV). The experimental results showed that the potassium mono and di phosphates could insert into the BSA and quench the inner fluorescence of BSA by forming the potassium mono phosphate—BSA and pottassium di phosphate—BSA complexes. It was found that the static quenching was the main reason leading to the fluorescence quenching. It was conformed by XRD and SEM techniques.

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Authors and Affiliations

  1. Department of Physics, Annamalai University, Annamalainagr, 608 002, Tamilnadu, India

    S. Bakkialakshmi & D. Chandrakala

  2. Centralized Instrumentation and Services Laboratory (CISL), Annamalai University, Annamalainagar, 608 002, India

    B. Shanthi

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  1. S. Bakkialakshmi
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  2. B. Shanthi
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  3. D. Chandrakala
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Correspondence to S. Bakkialakshmi.

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Bakkialakshmi, S., Shanthi, B. & Chandrakala, D. Interaction of Potassium Mono and Di Phosphates with Bovine Serum Albumin Studied by Fluorescence Quenching Method. J Fluoresc 21, 687–692 (2011). https://doi.org/10.1007/s10895-010-0756-4

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  • DOI: https://doi.org/10.1007/s10895-010-0756-4

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