Abstract
Acid proteinases of the brain were isolated by gel filtration on a column with Sephadex G-100. Three peaks of enzyme activity were found. Cathepsin D with high molecular weight (over 150,000) is solubilized from brain tissues by 0.1% Triton X-100. Cathepsin D with a molecular weight of 59,000 is solubilized only by a 0.2% solution of the detergent. Low-molecular-weight (20,000) cathepsin D is a soluble cytoplasmic enzyme. The results are regarded as proof of the heterogeneity of molecular forms of acid proteinases in the cerebral cortex, corresponding to the strength of the bond between the enzymes and subcellular structure of brain tissue.
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Stepchenko, L.M., Berezin, V.A., Reva, A.D. et al. Molecular forms of acid brain proteinases. Bull Exp Biol Med 80, 1179–1180 (1975). https://doi.org/10.1007/BF00833152
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DOI: https://doi.org/10.1007/BF00833152