Bovine cathepsins S and L: isolation and amino acid sequences.
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.
Dolenc
I
I
Dept. of Biochemistry, J. Stefan Institute, Ljubljana, Slovenia.
Ritonja
A
A
Colić
A
A
Podobnik
M
M
Ogrinc
T
T
Turk
V
V
D000595:Amino Acid Sequence; D000818:Animals; D056668:Cathepsin L; D002403:Cathepsins / Q000032:analysis / Q000302:isolation & purification*; D002417:Cattle; D002852:Chromatography, Ion Exchange; D003546:Cysteine Endopeptidases; D004591:Electrophoresis, Polyacrylamide Gel; D010450:Endopeptidases; D007525:Isoelectric Focusing; D007668:Kidney / Q000201:enzymology; D008969:Molecular Sequence Data; D013154:Spleen / Q000201:enzymology
D002403:Cathepsins; D010450:Endopeptidases; D003546:Cysteine Endopeptidases; D056668:Cathepsin L; C028217:cathepsin S