Nagamatsu K, Suzuki K, Teshima R, Ikebuchi H, Terao T
National Institute of Hygienic Sciences, Tokyo, Japan.
Biochem J. 1989 Jan 1;257(1):165-71. doi: 10.1042/bj2570165.
Morphine and [D-Ala2,D-Leu5]enkephalinamide enhance the phosphorylation of a 58 kDa protein in mouse brain synaptosomal membranes. The enhancement of phosphorylation was inhibited by naloxone, an antagonist of morphine. The phosphorylated 58 kDa protein was retained on wheat-germ-agglutinin-agarose and morphinone-Affi-Gel 401 columns and biospecifically eluted out from the columns with N-acetyl-D-glucosamine and naloxone respectively. These results suggest a strong possibility that the opiate-binding protein undergoes phosphorylation by endogenous protein kinase. Since the molecular mass of a mu-type opioid receptor in mouse brain is suggested to be 58 kDa, coincident with those of rat brain and neuroblastoma x glioma hybrid cells, it is conceivable that the phosphorylated 58 kDa protein is a mu-type receptor.
吗啡和[D-丙氨酸2，D-亮氨酸5]脑啡肽酰胺能增强小鼠脑突触体膜中一种58 kDa蛋白质的磷酸化作用。磷酸化作用的增强被吗啡拮抗剂纳洛酮所抑制。磷酸化的58 kDa蛋白质保留在麦胚凝集素-琼脂糖柱和吗啡酮-Affi-Gel 401柱上，并分别用N-乙酰-D-葡糖胺和纳洛酮从柱上进行生物特异性洗脱。这些结果提示阿片类结合蛋白极有可能被内源性蛋白激酶磷酸化。由于小鼠脑中μ型阿片受体的分子量被认为是58 kDa，与大鼠脑和神经母细胞瘤x胶质瘤杂交细胞的分子量一致，可以推测磷酸化的58 kDa蛋白质是μ型受体。
