Author/Editor		Dolenc, I; Ritonja, A; Čolič, A; Podobnik, M; Ogrinc, T; Turk, V
Title		Bovine cathepsins S and L: isolation and amino acid sequences
Type		članek
Source		Biol Chem Hoppe Seyler
Vol. and No.		Letnik 373, št. 7
Publication year		1992
Volume		str. 407-12
Language		eng
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.
Descriptors		CATHEPSINS AMINO ACID SEQUENCE CATHEPSINS CATTLE CHROMATOGRAPHY, ION EXCHANGE ELECTROPHORESIS, POLYACRYLAMIDE GEL ISOELECTRIC FOCUSING KIDNEY MOLECULAR SEQUENCE DATA SPLEEN