Kovaleva I E, Novikova L A, Luzikov V N
Belozersky Laboratory of Molecular Biology and Bioorganic Chemistry, Moscow State University, USSR.
FEBS Lett. 1989 Jul 17;251(1-2):183-6. doi: 10.1016/0014-5793(89)81451-6.
Alpha-amylase from Bacillus amyloliquefaciens, synthesized in yeast Saccharomyces cerevisiae without substitution of the signal sequence, is efficiently secreted from yeast cells: 60-70% of the overall amount of the enzyme is found in the culture fluid. In contrast to many yeast secretory proteins, which accumulate in the periplasmic space and in the cell wall, intracellular alpha-amylase is localized mainly in the cytoplasm. Obviously, transfer across the cell wall is not a rate-limiting step in alpha-amylase export from the cell. The glycosylated forms of proteins are predominantly found both inside the cell and in the culture medium.
在酿酒酵母中合成的解淀粉芽孢杆菌α淀粉酶，未替换信号序列，能有效从酵母细胞中分泌：培养液中可发现该酶总量的60%-70%。与许多在周质空间和细胞壁中积累的酵母分泌蛋白不同，细胞内α淀粉酶主要定位于细胞质中。显然，穿过细胞壁并非α淀粉酶从细胞中输出的限速步骤。糖基化形式的蛋白质主要存在于细胞内和培养基中。
