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A circular dichroism and fluorescence spectrometric assessment of effects of selected chemical denaturants on soybean (Glycine max L.) storage proteins glycinin (11S) and beta-conglycinin (7S).

A circular dichroism and fluorescence spectrometric assessment of effects of selected chemical denaturants on soybean (Glycine max L.) storage proteins glycinin (11S) and beta-conglycinin (7S). Research Abstract Details 

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  • A circular dichroism and fluorescence spectrometric assessment of effects of selected chemical denaturants on soybean (Glycine max L.) storage proteins glycinin (11S) and beta-conglycinin (7S). Abstract Text:

    k w clara szeK W Clara Sze,harshal h kshirsagarHarshal H Kshirsagar,mahesh venkatachalamMahesh Venkatachalam,shridhar k satheShridhar K Sathe,k w clara szeK W Clara Sze,harshal h kshirsagarHarshal H Kshirsagar,mahesh venkatachalamMahesh Venkatachalam,shridhar k satheShridhar K Sathe,

    Soybean glycinin (11S) and beta-conglycinin (7S) were subjected to select chemical treatments at various concentrations and resulting changes in protein structures were investigated by circular dichroism (CD) and fluorescence spectrometry. Fluorescence quenching results indicated that urea >/=3 M caused significant unfolding of 11S, but not that of 7S. GuHCl was more effective than urea in denaturation of 11S. A two-step transition in 11S structure was observed with a possible existence of a folding intermediate at 2.5 M GuHCl. Sodium dodecyl sulfate (SDS) measurably altered secondary and tertiary structures of 11S and 7S below SDS critical micellar concentration (CMC), possibly due to formation of mixed peptide-SDS micelles. SDS treatment increased alpha-helical and unordered structures of both proteins at the expense of beta-sheet structure. NaCl and CaCl 2 caused a significant decrease in fluorescence intensity without shifting emission lambda max. Exposure of 7S and 11S to NaSCN respectively at >/=0.3 and >/=0.6 M NaSCN caused a significant increase in fluorescence intensity measured at the corresponding lambda max of the protein. beta-Mercaptoethanol (beta-ME), N-ethylmaleimide (NEM), and phytic acid caused variable red shifts, 2.5-4 nm, in the emission lambda max.

    A circular dichroism and fluorescence spectrometric assessment of effects of selected chemical denaturants on soybean (Glycine max L.) storage proteins glycinin (11S) and beta-conglycinin (7S). Publishing Authors By Initials

    kw clara szeKW Clara Sze,hh kshirsagarHH Kshirsagar,m venkatachalamM Venkatachalam,sk satheSK Sathe,kw clara szeKW Clara Sze,hh kshirsagarHH Kshirsagar,m venkatachalamM Venkatachalam,sk satheSK Sathe,

    For similar organic chemicals: urea research abstracts see: organic chemicals: urea research

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    A circular dichroism and fluorescence spectrometric assessment of effects of selected chemical denaturants on soybean (Glycine max L.) storage proteins glycinin (11S) and beta-conglycinin (7S). Journal Published:

    PUBLICATION TYPE: Research Support, Non-U.S. Gov

    Journal: Journal of agricultural and food chemistry

    VOLUME: 55

    Page Numbers: 8745-53

    Journal Abbreviation: J. Agric. Food Chem.

    ISSN: 0021-8561

    DAY: 20

    MONTH: 09

    YEAR: 2007

    A circular dichroism and fluorescence spectrometric assessment of effects of selected chemical denaturants on soybean (Glycine max L.) storage proteins glycinin (11S) and beta-conglycinin (7S). Information

    Number of References:

    LANGUAGE: eng

    NlmUniqueID: 374755

    A circular dichroism and fluorescence spectrometric assessment of effects of selected chemical denaturants on soybean (Glycine max L.) storage proteins glycinin (11S) and beta-conglycinin (7S). Keywords Mesh Terms:

    KEYWORDS: Urea

    MESH TERMS: pharmacology

    Chemical & Substance for Abstract: A circular dichroism and fluorescence spectrometric assessment of effects of selected chemical denaturants on soybean (Glycine max L.) storage proteins glycinin (11S) and beta-conglycinin (7S). Information

    Substance Name: glycinin

    Registry Number: 9007-93-6

    Grant and Affiliation Information for A circular dichroism and fluorescence spectrometric assessment of effects of selected chemical denaturants on soybean (Glycine max L.) storage proteins glycinin (11S) and beta-conglycinin (7S).

    AFFILIATION: Department of Nutrition, Food & Exercise Sciences, College of Human Sciences, Florida State University, Tallahassee, Florida 32306-1493, USA. ssathe@mailer.fsu.edu

    Country: United States

    United States Research PublicationUnited States Research Publication

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    MEDLINETA: J Agric Food Chem

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    A circular dichroism and fluorescence spectrometric assessment of effects of selected chemical denaturants on soybean Glycine max L storage proteins glycinin 11S and beta-conglycinin 7S Related Publications

     

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