Abstract
Gel permeation chromatography fractions of short-chain peptides from a hydrolysate product, which in turn was from the purified porcine brain through enzyme hydrolysis, were tested for their biological activities. The results showed that the fractions A4 and A5 had significant biological activities. The two fractions were analyzed with analytical techniques such as high-performance liquid chromatography (HPLC), capillary zone electrophoresis (CZE), isoelectric focusing (IEF), discontinuous sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE). Preliminary results showed that the main components of these two fractions were short-chain acidic peptides with a relative molecular mass ( M r) of less than 2400.
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