Buckmaster M J, Ferris A L, Storrie B
Department of Biochemistry and Nutrition, Virginia Polytechnic Institute and State University, Blacksburg 24061.
Biochem J. 1988 Feb 1;249(3):921-3. doi: 10.1042/bj2490921.
Upon detergent or hypo-osmotic lysis of CHO-cell postnuclear supernatants or isolated lysosomes at pH 4.8, the lysosomal enzymes beta-hexosaminidase, beta-galactosidase, alpha-fucosidase and cathepsin C were readily pelleted, whereas the exogenous marker, long-term-internalized horseradish peroxidase, was not. Salt or pH elevation greatly decreased lysosomal-enzyme pelletability. The results suggest that, under native conditions, lysosomal hydrolases may be aggregated. Aggregation could promote enzyme retention within the organelle.
在pH 4.8条件下,对CHO细胞的核后上清液或分离的溶酶体进行去污剂或低渗裂解时,溶酶体酶β-己糖胺酶、β-半乳糖苷酶、α-岩藻糖苷酶和组织蛋白酶C很容易沉淀,而外源性标记物、长期内化的辣根过氧化物酶则不会。盐浓度升高或pH值升高会大大降低溶酶体酶的沉淀能力。结果表明,在天然条件下,溶酶体水解酶可能会聚集。聚集可能会促进酶保留在细胞器内。