Weller M, Morgan I G
Biochim Biophys Acta. 1977 Mar 17;465(3):527-34. doi: 10.1016/0005-2736(77)90270-x.
Incubation of synaptosomes under conditions which result in complete phosphorylation of membrane bound accepter proteins does not affect the permeability to Na+ or K+ as measured by a spectrophotometric method. This technique was not, however, sensitive enough to determine permeability to Ca2+ which was thus estimated, using 45Ca2+. It was found that although phosphorylation did not affect the equilibrium binding of 45Ca it did lower the rate of both Ca2+ uptake and efflux. The most likely interpretation of these results is that phosphorylation of proteins in the synaptic membrane lowers the permeability of the membrane to Ca2+. This could have a role in the regulation of synaptic transmission.
在能使膜结合受体蛋白完全磷酸化的条件下孵育突触体，通过分光光度法测量，这并不会影响其对Na⁺或K⁺的通透性。然而，这项技术对于测定Ca²⁺的通透性不够灵敏，因此使用⁴⁵Ca²⁺来估计Ca²⁺的通透性。结果发现，尽管磷酸化并不影响⁴⁵Ca的平衡结合，但它确实降低了Ca²⁺摄取和外流的速率。对这些结果最合理的解释是，突触膜中蛋白质的磷酸化降低了膜对Ca²⁺的通透性。这可能在突触传递的调节中起作用。
