Possibilities and pitfalls in quantifying the extent of cysteine sulfenic acid modification of specific proteins within complex biofluids |
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Authors: | Douglas S Rehder Chad R Borges |
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Institution: | (1) Molecular Biomarkers, The Biodesign Institute at Arizona State University, Tempe, AZ 85287, USA |
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Abstract: | Background Cysteine sulfenic acid (Cys-SOH) plays important roles in the redox regulation of numerous proteins. As a relatively unstable
posttranslational protein modification it is difficult to quantify the degree to which any particular protein is modified
by Cys-SOH within a complex biological environment. The goal of these studies was to move a step beyond detection and into
the relative quantification of Cys-SOH within specific proteins found in a complex biological setting--namely, human plasma. |
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