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- W1967133021 abstract "Procedures are described for extraction or release, assay and purification of cerebrocystatin an inhibitor of brain cathepsin B or of papain. Neurosecretory regions of rat brain contained significantly higher amounts of cerebrocystatin compared to cortex, cerebellum, mid- and lower brain regions, and spinal cord. Inhibitor was purified to apparent homogeneity by alkaline treatment of rat brain cytosol, followed by gel-filtration and affinity chromatography on Reacti-gel coupled to alkylated papain. Purified cerebrocystatin was a single polypeptide of Mr 12,500 as shown by gel-electrophoresis on urea-SDS slab gels. Cerebrocystatin inhibited the hydrolysis of BANA by papain (Ki, 1 nM) or by purified rat brain cathepsin B (Ki, 10 nM) and suppressed the hydrolysis of myelin basic protein (MBP) by cathepsin B (I50, 0.8 microM) and prevented its cleavage to form polypeptides of Mr 15,000-17,000." @default.
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- W1967133021 date "1983-05-01" @default.
- W1967133021 modified "2023-09-26" @default.
- W1967133021 title "Cerebrocystatin suppresses degradation of myelin basic protein by purified brain cysteine proteinase" @default.
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- W1967133021 doi "https://doi.org/10.1016/0006-291x(83)91717-5" @default.
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