Fayet Y, Degiuli A, Got R, Frot-Coutaz J
Laboratoire de Biochimie des Membranes, UM 380024, Université Claude-Bernard, Lyon I, Villeurbanne, France.
Biochimie. 1988 Jun;70(6):735-42. doi: 10.1016/0300-9084(88)90102-2.
A retinylphosphate binding activity, resolved during purification, has been discovered in rat liver cytosol. The partial purification includes ammonium sulfate precipitation and DEAE-cellulose chromatography. The macromolecular component responsible for the binding has a sedimentation coefficient of about 2 S and is sensitive to pronase. This binding is reversible and specific for retinylphosphate, since retinol, retinoic acid and retinoylphosphate do not compete with [3H]retinylphosphate.
在大鼠肝脏胞质溶胶中发现了一种在纯化过程中得以分离的视黄基磷酸结合活性。部分纯化过程包括硫酸铵沉淀和二乙氨基乙基纤维素色谱法。负责该结合的大分子成分沉降系数约为2S，且对链霉蛋白酶敏感。这种结合是可逆的，对视黄基磷酸具有特异性，因为视黄醇、视黄酸和视黄酰磷酸不与[3H]视黄基磷酸竞争。
