Salpeter M M
J Cell Biol. 1967 Feb;32(2):379-89. doi: 10.1083/jcb.32.2.379.
Tritiated diisopropylfluorophosphate (DFP) was used to phosphorylate acetylcholinesterase (AChase) in the motor end plate of mouse sternomastoid muscle, and its distribution within the end plate was evaluated quantitatively by electron microscope radioautography. With the use of emulsion layers whose sensitivity to tritium had been calibrated, the density of AChase in different components of the end plate was calculated. The AChase was primarily localized (85%) in the junctional fold region. The concentration of AChase there was more than 20,000 active sites per cubic micron of tissue. The resolution of the technique was not sufficient to determine whether there was some AChase in the nerve end bulb; however, if there is any there, the concentration must be less than 10% of that at the junctional fold region.
用氚标记的二异丙基氟磷酸酯(DFP)对小鼠胸锁乳突肌运动终板中的乙酰胆碱酯酶(AChase)进行磷酸化,并通过电子显微镜放射自显影法定量评估其在终板内的分布。使用对氚敏感性已校准的乳剂层,计算终板不同成分中AChase的密度。AChase主要定位于(85%)连接褶区域。该区域每立方微米组织中AChase的浓度超过20000个活性位点。该技术的分辨率不足以确定神经末梢球中是否存在一些AChase;然而,如果那里存在任何AChase,其浓度必定低于连接褶区域浓度的10%。