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- W2327287844 abstract "The purification procedure of cathepsin S includes acid activation of spleen homogenate, incubation at 37 degrees C, precipitation with (NH4)2SO4 in H2O/tert-butanol medium, gel chromatography, chromatofocusing, covalent chromatography and cation chromatography of FPLC system. Cathepsin S has a M(r) of about 24,000 Da with pI of 6.5 and 6.8. The mixture of both forms gave a single sequence. Cathepsin L was purified from bovine kidney by acid treatment and incubation of 37 degrees C, precipitation by (NH4)2SO4, two ion exchange chromatographies on CM-Sephadex, gel chromatography and ion exchange chromatography on FPLC system. Cathepsin L exists in multiple forms with pI 5.3-5.7 and M(r) of about 29,000 Da. N-terminal amino acid sequence confirms that cathepsin L and cathepsin S are different enzymes." @default.
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- W2327287844 date "1992-01-01" @default.
- W2327287844 modified "2023-10-18" @default.
- W2327287844 title "Bovine Cathepsins S and L: Isolation and Amino Acid Sequences" @default.
- W2327287844 cites W1775749144 @default.
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- W2327287844 doi "https://doi.org/10.1515/bchm3.1992.373.2.407" @default.
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