Barnes K, Turner A J, Kenny A J
Department of Biochemistry, University of Leeds, U.K.
Neurosci Lett. 1988 Nov 22;94(1-2):64-9. doi: 10.1016/0304-3940(88)90271-6.
An ultrastructural study of endopeptidase-24.11 in the globus pallidus from the brain of a newborn pig is reported. The antigen was localized by an immunoperoxidase method using an affinity-purified polyclonal antibody in which staining was performed on thick vibratome sections prior to osmication and flat embedding. When areas selected by light microscopy for re-embedding were examined in the electron microscope a minority of the axonal membranes in the fields examined were observed to be immunostained for endopeptidase-24.11. These were unmyelinated fibres and the membrane staining included not only the length of an axon but also some boutons synapsing with dendrites. Positively staining dendritic and glial membranes were not observed. These results support the view that endopeptidase-24.11 may play a role in inactivating some neuropeptides after their release at the synapse.
报道了对新生猪脑苍白球中内肽酶-24.11的超微结构研究。使用亲和纯化的多克隆抗体，通过免疫过氧化物酶方法对抗原进行定位，其中在锇化和扁平包埋之前，在厚振动切片上进行染色。当在电子显微镜下检查通过光学显微镜选择用于重新包埋的区域时，在所检查的视野中观察到少数轴突膜对内肽酶-24.11呈免疫染色。这些是无髓纤维，膜染色不仅包括轴突的长度，还包括一些与树突形成突触的终扣。未观察到树突膜和胶质细胞膜呈阳性染色。这些结果支持这样一种观点，即内肽酶-24.11可能在某些神经肽在突触处释放后使其失活中发挥作用。
