Vihko P, Wahlberg L, Ehnholm C, Lukka M, Vihko R
FEBS Lett. 1986 Jul 7;202(2):309-13. doi: 10.1016/0014-5793(86)80707-4.
The serum protein binding secretory prostatic acid phosphatase (PAP) and lysosomal placental acid phosphatase (LAP) was purified using affinity chromatography on gels containing immobilized acid phosphatases. The protein, which could be eluted from these enzyme affinity gels only with 0.05 mol/l HCl (pH 2.0), was shown to be apolipoprotein A-I (apo A-I), the main structural protein of high density lipoprotein (HDL).
使用固定化酸性磷酸酶的凝胶亲和层析法纯化血清蛋白结合分泌型前列腺酸性磷酸酶(PAP)和溶酶体胎盘酸性磷酸酶(LAP)。结果表明,仅能用0.05mol/L盐酸(pH2.0)从这些酶亲和凝胶上洗脱下来的蛋白质是载脂蛋白A-I(apo A-I),即高密度脂蛋白(HDL)的主要结构蛋白。