Gruppo di Chimica Biologica e Strutturistica Chimica della Facoltà di Scienze, Università di Roma "La Sapienza", Città Universitaria, I-00185, Rome, Italy.
Planta. 1984 Apr;160(5):422-7. doi: 10.1007/BF00429758.
The poor stability of crude solutions of fusicoccin-binding sites, prepared from acetonedried microsomal fractions of spinach leaves, results from the attack by endogenous phosphatase and α-mannosidase. The addition of either of these enzymes to solubilised binding sites preincubated with [(3)H]fusicoccin promptly releases most of the bound radioactivity. A satisfactory stabilization of the crude preparations is obtained with fluoride added either during homogenization of the tissue, or immediately after solubilisation. The results indicate that the fusicoccin-binding sites are phosphorylated glycoproteins.
从菠菜叶片的丙酮干燥微粒体部分制备的 Fusicoccin 结合部位的粗溶液稳定性差，这是由于内源性磷酸酶和α-甘露糖苷酶的攻击所致。将这些酶中的任一种添加到与 [(3)H]Fusicoccin 预孵育的溶解结合部位中，会迅速释放出大部分结合的放射性。通过在组织匀浆过程中或在溶解后立即添加氟化物，可以对粗制剂进行令人满意的稳定。结果表明，Fusicoccin 结合部位是磷酸化糖蛋白。
