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A Tailored HPLC Purification Protocol That Yields High-purity Amyloid Beta 42 and Amyloid Beta 40 Peptides, Capable of Oligomer Formation
Published on: March 27, 2017
Purification and characterization of alpha 1-antichymotrypsin from human pleural fluid and human serum
Abstract:
Human alpha 1-antichymotrypsin was purified from human pleural fluid and from human serum. Four affinity chromatographic steps were required to obtain pure alpha 1-antichymotrypsin. Pleural and serum alpha 1-antichymotrypsin have the same molecular weight, which was estimated by SDS-polyacrylamide gel electrophoresis to be 58 000. The chemical composition of the two types of alpha 1-antichymotrypsin is the same. Using a technique for visualization of the chymotrypsin inhibitors, we showed that the pure alpha 1-antichymotrypsin obtained from the two physiological fluids had its inhibitory capacity preserved.

