Journal
SPECTROCHIMICA ACTA PART A-MOLECULAR AND BIOMOLECULAR SPECTROSCOPY
Volume 72, Issue 3, Pages 682-685Publisher
PERGAMON-ELSEVIER SCIENCE LTD
DOI: 10.1016/j.saa.2008.10.058
Keywords
Bovine serum albumin; Soybean isoflavone; Fluorescence quenching; Hydroxylation and glycosylation
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In this paper, the influence of hydroxylation and glycosylation of soybean isoflavones in ring A on the interaction with BSA was investigated. Two soybean isoflavone aglycones (daidzein and genistein) and their glycosides (daidzin and genistin) were used to study their ability to bind BSA by quenching the BSA intrinsic fluorescence in solution. The hydroxylation and glycosylation of soybean isoflavones in ring A significantly affected the binding/quenching process; in general, the hydroxylation increases the binding affinity and the glycosylation decreased the binding affinity. For daidzein and daidzin, the binding constants for BSA were 5.2 x 10(4) and 5.58 x 10(3) L mol(-1), respectively. For genistein and genistin, the binding constants were 8.40 x 10(5) and 1.44 x 10(5) Lmol(-1), respectively. (c) 2008 Elsevier B.V. All rights reserved.
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