Abstract
Trichloboacetic acid has been used for denaturing and removing inert tissue proteins from kidney extracts containing renin1. It is also known that agents commonly used for removing proteins from solutions precipitate the proteins without causing denaturation in certain cases, so that the original protein may be regained. Thus trypsin and trypsinogen can be precipitated with trichloroacetic acid and the active enzymes regained2. In the same manner, crystalline egg albumin can be precipitated with metaphosphoric acid3 and cathepsin by tungstic acid4.
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References
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ASTRUP, T., BIRCH-ANDERSEN, A. Purification of Renin by Means of Protein-Precipitating Agents. Nature 160, 570–571 (1947). https://doi.org/10.1038/160570b0
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DOI: https://doi.org/10.1038/160570b0
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