Honchar M P, Bunge M B, Agrawal H C
Neurochem Res. 1982 Apr;7(4):365-72. doi: 10.1007/BF00965490.
Neurofilament proteins from brain and spinal cord of immature rat (20-35 days of age) and rabbit (15-17) days of age) were prepared by an axonal flotation technique. Examination of rat filament preparations by electron microscopy revealed a preponderance of 10 nm diameter filaments that were usually loosely aggregated although some bundles of more tightly packed filaments were present as well. The neurofilament triplet proteins of the rat and rabbit central nervous system were found to be phosphorylated 24 hr after the intracerebral injection of [32P]orthophosphate when examined by sodium dodecyl sulfate polyacrylamide gel electrophoresis followed by fluorography. Examination of each eluted neurofilament protein from both species showed that [32P]phosphate was retained after reelectrophoresis and fluorography. Evidence is presented that the [32P]phosphate is covalently linked to the purified neurofilament proteins by phosphoester bonds.
采用轴突漂浮技术制备了未成熟大鼠（20 - 35日龄）和兔（15 - 17日龄）脑和脊髓中的神经丝蛋白。通过电子显微镜检查大鼠神经丝制剂发现，直径为10 nm的细丝占优势，这些细丝通常松散聚集，不过也存在一些紧密堆积的细丝束。当通过十二烷基硫酸钠聚丙烯酰胺凝胶电泳随后进行荧光自显影检查时，发现大鼠和兔中枢神经系统的神经丝三联体蛋白在脑内注射[32P]正磷酸盐24小时后发生了磷酸化。对两种动物洗脱的每种神经丝蛋白进行检查表明，再电泳和荧光自显影后[32P]磷酸盐仍保留。有证据表明，[32P]磷酸盐通过磷酸酯键与纯化的神经丝蛋白共价连接。
