Conformational State of Disulfide-Reduced Ovalbumin at Acidic pH
نویسندگان
چکیده
منابع مشابه
Monomeric Banana Lectin at Acidic pH Overrules Conformational Stability of Its Native Dimeric Form
Banana lectin (BL) is a homodimeric protein categorized among jacalin-related family of lectins. The effect of acidic pH was examined on conformational stability of BL by using circular dichroism, intrinsic fluorescence, 1-anilino-8-napthalene sulfonate (ANS) binding, size exclusion chromatography (SEC) and dynamic light scattering (DLS). During acid denaturation of BL, the monomerization of na...
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To investigate the highly denatured state of ovalbumin (molecular mass of 42.7 kDa, four cysteine sulfhydryls and one cystine disulfide) using the disulfide rearrangement approach, we established the peptide-mapping procedure using a cysteine-labeling technique with a fluorescent dye that allows the quantitative analyses for the disulfide-involved half-cystines. Ovalbumin denatured at a low pro...
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Sulfhydryl groups of ovalbumin were chemically modified under denaturing conditions in the absence and presence of dithiothreitol, and effects on the secondary structure of the protein were investigated by circular dichroic (CD) measurements. The contents of alpha-helix, beta-structure, and "random coil" (unordered, nonrepetitive structure) were estimated by simulation of the CD spectra and usi...
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ژورنال
عنوان ژورنال: Bioscience, Biotechnology, and Biochemistry
سال: 1999
ISSN: 0916-8451,1347-6947
DOI: 10.1271/bbb.63.1285