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- W2043030894 abstract "The precipitation of lysozyme at 60°C in pH 9.2 buffer solution followed first-order kinetics. The first-order rate constants varied with initial protein concentration possibly due to nonpurity. Heat precipitation of bovine serum albumin (BSA) in pure water did not follow any simple rate law but in pH 5.8 buffer obeyed first-order kinetics in the initial stages.The extent of aggregation of BSA in the precipitate was followed by dissolving the precipitate in acid solution with subsequent characterization by gel-permeation chromatography. Addition of small amounts of the sulfhydryl blocking agent, iodoacetamide (twelve times the concentration of protein on a molar basis), reduced the aggregation. Heat precipitation of proteins appears to be governed by the favorable entropy change when interactions between water molecules and nonpolar groups of the protein are decreased." @default.
- W2043030894 created "2016-06-24" @default.
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- W2043030894 date "2007-03-08" @default.
- W2043030894 modified "2023-10-09" @default.
- W2043030894 title "Kinetics of heat precipitation of proteins" @default.
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- W2043030894 doi "https://doi.org/10.1002/polc.5070550115" @default.
- W2043030894 hasPublicationYear "2007" @default.
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