Interaction of human cathepsin C with chicken cystatin
- 2 September 1996
- journal article
- Published by Wiley in FEBS Letters
- Vol. 392 (3) , 277-280
- https://doi.org/10.1016/0014-5793(96)00828-9
Abstract
Cathepsin C was purified from human spleen by a rapid procedure, which included homogenization, ammonium sulfate precipitation, gel filtration on Sephacryl S-200 and finally affinity chromatography on chicken cystatin-Sepharose. The interaction between cathepsin C and chicken cystatin was further characterized. It was found to be accompanied by a maximum decrease in fluorescence emission intensity at 330 nm. Fluorescence titration showed that human cathepsin C can bind four chicken cystatin molecules. The 4:1 binding stoichiometry was confirmed by titration monitored by the loss of enzyme activity. A non-competitive-competitive type of inhibition was determined from a double-reciprocal Lineweaver-Burk plot with a K i value of 0.22 nM for the non-competitive inhibition.Keywords
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