Komine S, Nakanishi K, Anzai T, Yoshimoto A
Cell Biochem Funct. 1985 Jan;3(1):41-4. doi: 10.1002/cbf.290030109.
We previously reported that alpha-lactalbumin combines with the lysosomal membrane of mammary epithelial cells and that it acts to release lysosomal enzymes. However, the details of this combination within the cells remained undetermined. We now report that 125I-bovine-alpha-lactalbumin in the medium entered mouse mammary epithelial cells, and about 13 per cent of the alpha-lactalbumin that entered the cell bound to lysosomes. About 75 per cent of the alpha-lactalbumin that reached the lysosome was tightly bound to the lysosomal membrane. It appears that alpha-lactalbumin in the secretory vesicles does not migrate out, because murine and bovine whey did not induce the release of Golgi enzymes in vitro.
我们之前报道过，α-乳白蛋白与乳腺上皮细胞的溶酶体膜结合，并起到释放溶酶体酶的作用。然而，这种在细胞内结合的细节仍未确定。我们现在报道，培养基中的125I-牛α-乳白蛋白进入了小鼠乳腺上皮细胞，进入细胞的α-乳白蛋白约有13%与溶酶体结合。到达溶酶体的α-乳白蛋白约75%紧密结合在溶酶体膜上。似乎分泌小泡中的α-乳白蛋白不会迁移出来，因为鼠乳清和牛乳清在体外不会诱导高尔基体酶的释放。
