Mikol D D, Stefansson K
Department of Neurology, University of Chicago, Illinois 60637.
J Cell Biol. 1988 Apr;106(4):1273-9. doi: 10.1083/jcb.106.4.1273.
Here we report the isolation and initial biochemical characterization of a 120-kD peanut agglutinin-binding glycoprotein from the adult human central nervous system (CNS), which is anchored to membranes through a phosphatidylinositol linkage. Myelin incubated with phosphatidylinositol-specific phospholipase C released the protein as a soluble polypeptide of 105 kD, which was isolated with peanut agglutinin-agarose affinity chromatography. The protein was found to be highly glycosylated. The protein appears to be confined to the CNS, where its developmental expression is region specific and parallels myelination. It is in greater quantity in white matter than in gray matter and it is in isolated human CNS myelin. Furthermore, ovine oligodendrocytes in culture contain the protein on their surfaces and release it into the supernatant as a soluble 105-kD form. We call this protein the oligodendrocyte-myelin protein.
在此,我们报告了从成人中枢神经系统(CNS)中分离出一种120-kD花生凝集素结合糖蛋白,并对其进行了初步生化特性分析,该蛋白通过磷脂酰肌醇连接锚定在膜上。用磷脂酰肌醇特异性磷脂酶C处理髓磷脂,可释放出一种105 kD的可溶性多肽蛋白,该蛋白通过花生凝集素-琼脂糖亲和层析法分离得到。发现该蛋白高度糖基化。该蛋白似乎局限于中枢神经系统,其发育表达具有区域特异性,与髓鞘形成平行。在白质中的含量高于灰质,且存在于分离出的人中枢神经系统髓磷脂中。此外,培养的绵羊少突胶质细胞在其表面含有该蛋白,并以可溶性105-kD形式释放到上清液中。我们将这种蛋白称为少突胶质细胞-髓磷脂蛋白。