Opekarová M, Kotyk A, Horák J, Kholodenko V P
Eur J Biochem. 1975 Nov 15;59(2):373-6. doi: 10.1111/j.1432-1033.1975.tb02464.x.
Transfer of exponentially growing cells of Saccharomyces cerevisiae epsilon 1278 b to a fresh medium (or simply to distilled water) resulted in the loss of ability to transport arginine (and lysine), accompanied by the release of several proteins from the membrane surface or periplasmic space. Fractionation by ultrafiltration, Sephadex G-50 chromatography and freeze-drying yielded a homogeneous protein (55 mg per 100 g dry weight of cells) with specific binding ability for L-arginine (Kd = 3.8 X 10(-1) M) and L-lysine (Ki = 4.2 X 10(-4) M). The protein contains over 40 amino acid residues and has a molecular weight of about 5,000. In solution, it appears to aggregate as its concentration is raised, thereby decreasing the overall binding capacity for arginine. Addition of the protein to a depleted culture does not restore the transport of arginine. It is apparently the recognition protein for the specific arginine-transporting system of Saccharomyces cerevisiae but it occurs in almost identical amounts in the MG 168 mutant with impaired arginine transport.
将指数生长的酿酒酵母ε1278 b细胞转移至新鲜培养基（或仅转移至蒸馏水中）会导致其运输精氨酸（和赖氨酸）的能力丧失，同时伴随着几种蛋白质从膜表面或周质空间释放。通过超滤、葡聚糖G - 50色谱法和冷冻干燥进行分级分离，得到一种均质蛋白质（每100克细胞干重含55毫克），它对L - 精氨酸（解离常数Kd = 3.8×10⁻¹ M）和L - 赖氨酸（抑制常数Ki = 4.2×10⁻⁴ M）具有特异性结合能力。该蛋白质含有40多个氨基酸残基，分子量约为5000。在溶液中，随着浓度升高它似乎会聚集，从而降低对精氨酸的总体结合能力。将该蛋白质添加到耗尽的培养物中并不能恢复精氨酸的运输。它显然是酿酒酵母特异性精氨酸转运系统的识别蛋白，但在精氨酸运输受损的MG 168突变体中其含量几乎相同。
