Literature DB >> 21072683

Interaction of potassium mono and di phosphates with bovine serum albumin studied by fluorescence quenching method.

S Bakkialakshmi1, B Shanthi, D Chandrakala.   

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. © Springer Science+Business Media, LLC 2010

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Year:  2010        PMID: 21072683     DOI: 10.1007/s10895-010-0756-4

Source DB:  PubMed          Journal:  J Fluoresc        ISSN: 1053-0509            Impact factor:   2.217


  14 in total

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Journal:  Biophys J       Date:  1988-12       Impact factor: 4.033

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Journal:  Biochemistry       Date:  1993-07-27       Impact factor: 3.162

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10.  Methyl parathion interaction with human and bovine serum albumin.

Authors:  Dílson Silva; Célia M Cortez; Jayme Cunha-Bastos; Sônia R W Louro
Journal:  Toxicol Lett       Date:  2004-02-28       Impact factor: 4.372

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  2 in total

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