Activities of cathepsins A and D in cod muscle
β Scribed by R. McLay
- Publisher
- John Wiley and Sons
- Year
- 1980
- Tongue
- English
- Weight
- 241 KB
- Volume
- 31
- Category
- Article
- ISSN
- 0022-5142
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β¦ Synopsis
Abstract
Cathepsin A has been demonstrated in cod muscle. Cathepsins A and D were partially separated and purified from cod muscle. Cathepsin A and D are essentially similar to those from other sources. Cathepsin A acts optimally on the synthetic substrate CBZβΞ±βLβglutamylβLβtyrosine at pH 5.0, whereas cathepsin D hydrolyses haemoglobin optimally at pH 3.8. Cathepsin D did not hydrolyse the synthetic peptides acted upon by cathepsins A, B or C.
π SIMILAR VOLUMES
The aim of our study was to identify changes in secreted procathepsin B levels in a model of the human colorectal adenoma to carcinoma sequence and to determine the factors required for i t s extracellular activation. Conversion of the non-tumorigenic adenoma-derived cell line PC/AA to a highly tum