Hogue-Angeletti R A, Wu H L, Schlaepfer W W
J Neurochem. 1982 Jan;38(1):116-20. doi: 10.1111/j.1471-4159.1982.tb10861.x.
Intact neurofilaments were isolated from bovine spinal cord white matter, washed by sedimentation in 0.1 M-NaCl, and extracted with 8 M-urea. Solubilized neurofilament triplet proteins of molecular weights approximately 68,000 (P68), 150,000 (P150), and 200,000 (P200) were purified by preparative electrophoresis, using an LKB 7900 Uniphor apparatus. The method provides for an enhanced yield of purified protein and has markedly reduced admixture of electrophoresed protein with acrylamide and associated protein contaminants. Amino acid compositions of the purified neurofilament triplet proteins are reported and compared.
完整的神经丝从牛脊髓白质中分离出来，在0.1M氯化钠中通过沉降洗涤，并用8M尿素提取。分子量约为68,000（P68）、150,000（P150）和200,000（P200）的可溶性神经丝三联体蛋白通过制备电泳进行纯化，使用LKB 7900 Uniphor仪器。该方法提高了纯化蛋白的产量，并显著减少了电泳蛋白与丙烯酰胺及相关蛋白污染物的混合。报告并比较了纯化的神经丝三联体蛋白的氨基酸组成。
