"The inability to recover monomeric protein by heat treatment following the incubation of formaldehyde-treated proteins in ethanol may result from a combination of cross-link formation and a change in protein conformation. Thus, we examined the structural properties of RNase A treated with formaldehyde and ethanol using circular dichroism (CD) spectroscopy. The far-UV spectrum is sensitive to the secondary structure of the protein. Fixation in 10% formalin for up to 1 week did not significantly alter the secondary structure of RNase A relative to theuntreated protein. Additionally, native, unfixedRNase incubated in 100% ethanol for 1 week rapidly reverted back to as native structure after the ethanol was removed.
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Citation: Fowler CB, OâLearyTJ, MasonJT (2014) Improving the ProteomicAnalysis of Archival Tissue by Using Pressure-Assisted Protein Extraction:A Mechanistic Approach.J Proteomics Bioinform7: 151-157."
Last date updated on July, 2014