Literature DB >> 17158038

Spectroscopic probing of bile salt-albumin interaction.

Swati De1, Susmita Das, Agnishwar Girigoswami.   

Abstract

Interaction of the bile salts, sodium cholate and sodium deoxy cholate with albumin has been probed by fluorescence and circular dichroism studies. Both covalently and non-covalently labeled protein have been used to follow the aggregation of bile salts in presence of protein and to study bile salt-protein interactions in general. Time resolved studies, in agreement with steady-state fluorescence and circular dichroism studies, indicate alteration of protein secondary structure due to positive co-operative effects in bile salt binding to protein. These studies also indicate that covalent labeling may not always be good for studying proteins as it causes alteration of protein secondary structure.

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Year:  2006        PMID: 17158038     DOI: 10.1016/j.colsurfb.2006.09.015

Source DB:  PubMed          Journal:  Colloids Surf B Biointerfaces        ISSN: 0927-7765            Impact factor:   5.268


  2 in total

1.  Fluorescent probing of protein bovine serum albumin stability and denaturation using polarity sensitive spectral response of a charge transfer probe.

Authors:  Shalini Ghosh; Sankar Jana; Debnarayan Nath; Nikhil Guchhait
Journal:  J Fluoresc       Date:  2010-10-05       Impact factor: 2.217

2.  Denaturation studies on bovine serum albumin-bile salt system: Bile salt stabilizes bovine serum albumin through hydrophobicity.

Authors:  Karpagaraj Malarkani; Ivy Sarkar; Susithra Selvam
Journal:  J Pharm Anal       Date:  2017-06-23
  2 in total

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