Characterisation of the activity and stability of single-chain cathepsin L and of proteolytically active cathepsin L/cystatin complexes.
The activity of single-chain cathepsin L was found to be markedly dependent on cysteine concentration, while a covalent, proteolytically active cathepsin L/cystatin complex was less cysteine-dependent. Cysteine levels and ionic strength did not affect the stability of either enzyme form and both enzyme forms were found to be stable for significant periods of time at or near physiological pH.
Dennison
C
C
Department of Biochemistry, University of Natal, South Africa.
Pike
R
R
Coetzer
T
T
Kirk
K
K
D000818:Animals; D056668:Cathepsin L; D002403:Cathepsins / Q000032:analysis / Q000378:metabolism*; D002645:Chickens; D015891:Cystatins / Q000032:analysis / Q000378:metabolism*; D003545:Cysteine / Q000032:analysis; D003546:Cysteine Endopeptidases; D004591:Electrophoresis, Polyacrylamide Gel; D010450:Endopeptidases; D006863:Hydrogen-Ion Concentration; D008099:Liver / Q000201:enzymology; D012756:Sheep
D015891:Cystatins; D002403:Cathepsins; D010450:Endopeptidases; D003546:Cysteine Endopeptidases; D056668:Cathepsin L; D003545:Cysteine