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- W2225395880 abstract "The purpose of this study was (i) to generate proteolytic enzyme-derived fragments of murine alpha-fetoprotein (AFP); (ii) to characterize some of their physicochemical and immunological properties; and (iii) to isolate the fragments from proteolytic digests of mouse AFP. Significant differences in digestion patterns produced by the limited proteolysis of AFP were apparent. Proteolysis under denaturing conditions was most efficient and yielded smaller peptide fragments of narrower molecular weight range. Similar findings were observed for larger scale digests using milligram amounts of AFP. Some of the cleavage products were found to possess antigenic properties of the parent AFP molecule as demonstrated by immunoblotting experiments. Attempts were made to isolate individual AFP peptides from digests of 20-40 mg of the glycoprotein. Only partial separation of the proteolytic fragments was accomplished. Experiments were performed which involved testing the immunoregulatory activity of synthetic AFP peptides on an in vitro lymphocyte reaction known to be sensitive to AFP-mediated suppression. Anti-proliferative activity was observed with one of the peptides, AFP-34/48, which represents an amino acid sequence near the N-terminus of the parent molecule." @default.
- W2225395880 created "2016-06-24" @default.
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- W2225395880 date "1988-01-01" @default.
- W2225395880 modified "2023-09-27" @default.
- W2225395880 title "Analysis of proteolytic enzyme-derived fragments of murine alpha-fetoprotein" @default.
- W2225395880 hasPublicationYear "1988" @default.
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