Cathepsin S. The cysteine proteinase from bovine lymphoid tissue is distinct from cathepsin L (EC 3.4.22.15).

Abstract

Cathepsin S was purified from bovine spleen by acid autolysis, (NH4)2SO4 fractionation and chromatography on CM-Sephadex C-50, CM-cellulose and activated-thiol-Sepharose. Cathepsin L was isolated from lysosomal fractions of rat liver, rat kidney and bovine liver. Generally, cathepsin L was bound tightly to CM-Sephadex C-50. Preparations of cathepsin L from rat liver, rat kidney and bovine liver were shown to have kinetic constants for the substrate benzyloxycarbonyl-Phe-Arg-7-(4-methyl)coumarylamide in the same range (Km 2-3 microM). Benzyloxycarbonyl-Phe-Phe-diazomethane proved to be a sensitive irreversible inhibitor of cathepsin L from different species. Cathepsin S differed in all these characteristics from cathepsin L. A polyclonal antibody to cathepsin L from rat reacted with bovine cathepsin L but not with bovine cathepsin S.

• Authors: H Kirschke, I Schmidt, B Wiederanders
• Journal: The Biochemical journal (Biochem J) Vol. 240 Issue 2 Pg. 455-9 (Dec 01 1986) ISSN: 0264-6021 [Print] England
• PMID: 3814093 (Publication Type: Comparative Study, Journal Article)

Chemical References

• Antibodies
• Diazomethane
• benzyloxycarbonylphenylalanylphenylalanine diazomethyl ketone
• Cathepsins
• Endopeptidases
• Cysteine Endopeptidases
• Cathepsin L
• Ctsl protein, rat
• cathepsin S

Topics

• Animals
• Antibodies (analysis)
• Cathepsin L
• Cathepsins (antagonists & inhibitors, immunology, metabolism)
• Cattle
• Chromatography, Gel
• Cysteine Endopeptidases
• Diazomethane (analogs & derivatives, pharmacology)
• Electrophoresis, Polyacrylamide Gel
• Endopeptidases
• Kinetics
• Liver (enzymology)
• Molecular Weight
• Rats
• Spleen (enzymology)
• Substrate Specificity