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- W2061444250 abstract "Acylpeptide hydrolase, which removes the N-acetylated amino acids from peptide substrates was purified from bovine lens, truncated in vitro to a 55 kDa enzyme by trypsin digestion and characterized. The activity of the trypsin-modified enzyme was investigated using alpha A-crystallin and oxidized insulin A chain. The trypsin-modified enzyme was able to unblock alpha A-crystallin and displayed endoprotease activity unlike the native enzyme. SDS-PAGE analysis and amino acid sequencing of (3H)iPr2P-F labeled bovine lens acylpeptide hydrolase showed that the lens has a 55 kDa truncated form of the enzyme. The in vivo truncated form of the enzyme was generated by the cleavage of the Gly203-Asp204 peptide bond in the native enzyme." @default.
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- W2061444250 date "1998-06-01" @default.
- W2061444250 modified "2023-09-25" @default.
- W2061444250 title "Characterization of Trypsin-Modified Bovine Lens Acylpeptide Hydrolase" @default.
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- W2061444250 doi "https://doi.org/10.1006/bbrc.1998.8747" @default.
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