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A fluorescence study of human serum albumin binding sites modification by hypochlorite

Paper ID Volume ID Publish Year Pages File Format Full-Text
30391 44476 2009 5 PDF Available
Title
A fluorescence study of human serum albumin binding sites modification by hypochlorite
Abstract

A study has been made on the properties of human serum albumin (HSA) binding sites and how they are modified by pre-oxidation of the protein with hypochlorite. The oxidation extent was assessed from changes in the protein intrinsic fluorescence and production of carbonyl groups. HSA retains its solute binding capacity even after exposure to relatively large amounts of hypochlorite (up to 40 oxidant molecules per protein). From an analysis of the binding isotherms of dansyl sarcosine (DS) and dansyl-1-sulfonamide (DNSA) to native and hypochlorite treated albumin it is concluded that pre-oxidation of the protein reduces the number of active sites without affecting the binding capacity of the remaining binding sites. From DS and DNSA fluorescence anisotropy, Laurdan anisotropy and generalized polarization measurements, it is concluded that both Sites I and II in the native protein provide very rigid environments to the bound probes. These characteristics of the sites remain even after extensive treatment with hypochlorite. This stubbornness of HSA could allow the protein to maintain its function along its in vivo lifetime.

Keywords
Human serum albumin; Hypochlorite; Dansyl derivatives; Prodan
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A fluorescence study of human serum albumin binding sites modification by hypochlorite
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Publisher
Database: Elsevier - ScienceDirect
Journal: Journal of Photochemistry and Photobiology B: Biology - Volume 94, Issue 2, 9 February 2009, Pages 77–81
Authors
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Subjects
Physical Sciences and Engineering Chemical Engineering Bioengineering
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Don't Miss Today's Special Offer
Price was $35.95
You save - $31
Price after discount Only $4.95
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Full-text PDF Download
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