Characterisation of the Activity and Stability of Single-chain Cathepsin L and of Proteolytically Active Cathepsin L/Cystatin Complexes

Clive Dennison; Robert Pike; Theresa Coetzer; Kirsten Kirk

doi:10.1515/bchm3.1992.373.2.419

Characterisation of the Activity and Stability of Single-chain Cathepsin L and of Proteolytically Active Cathepsin L/Cystatin Complexes

Clive Dennison, Robert Pike, Theresa Coetzer, Kirsten Kirk

Research output: Contribution to journal › Article › Research › peer-review

14 Citations (Scopus)

Abstract

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.

Original language	English
Pages (from-to)	419-426
Number of pages	8
Journal	Biological Chemistry Hoppe-Seyler
Volume	373
Issue number	2
DOIs	https://doi.org/10.1515/bchm3.1992.373.2.419
Publication status	Published - 1 Jan 1992
Externally published	Yes

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10.1515/bchm3.1992.373.2.419

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AU - Kirk, Kirsten

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AB - 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.

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Characterisation of the Activity and Stability of Single-chain Cathepsin L and of Proteolytically Active Cathepsin L/Cystatin Complexes

Abstract

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