Liuzzi G M, Rizzo T, Ventola A, Riccio P, Quagliariello E
Dipartimento di Biochimica e Biologia Molecolare, Università di Bari, Italy.
Acta Neurol (Napoli). 1991 Apr;13(2):113-20.
Myelin basic protein (MBP) was purified from guinea pig spinal-cord in a native-like form retaining the binding to all the myelin lipids. Since the guinea pig MBP was found to be much more labile than the corresponding MBP from bovine brain, the original procedure based on the use of hydroxyapatite and detergents was slightly modified as reported here. The product of this purification, lipid-bound MBP, may represent an alternative to lipid-free MBP for the induction, the study and the treatment of experimental allergic encephalomyelitis.
髓鞘碱性蛋白（MBP）以一种类似天然的形式从豚鼠脊髓中纯化出来，保留了与所有髓鞘脂质的结合能力。由于发现豚鼠MBP比来自牛脑的相应MBP更不稳定，因此如本文所述，对基于使用羟基磷灰石和去污剂的原始方法进行了轻微修改。这种纯化产物，即脂质结合型MBP，可能是用于诱导、研究和治疗实验性过敏性脑脊髓炎的无脂质MBP的替代物。
