Lees M B, Chao B H, Laursen R A, L'Italien J J
Biochim Biophys Acta. 1982 Mar 18;702(1):117-24. doi: 10.1016/0167-4838(82)90034-6.
A hydrophobic, chloroform-soluble tryptic peptide with a molecular weight of approximately 4000 has been purified from the bovine white matter proteolipid protein. Its primary structure was obtained by a combination of solid-phase Edman degradation and mass spectrometry. A major part of the tryptic peptide appears to be inaccessible to the action of proteolytic enzymes. The peptide spans the three cyanogen bromide peptides located by Jollès et al. (Biochem. Biophys. Res. Commun. (1979) 87, 619--626) at the COOH-terminal region of the intact protein. Secondary structure calculations for this region indicate a segregation into discrete domains, with most of the tryptic peptide corresponding to a highly ordered, hydrophobic domain; an equal probability for alpha-helical or beta-structure is predicted for this region.
从牛脑白质蛋白脂蛋白中纯化出一种分子量约为4000的疏水性、可溶于氯仿的胰蛋白酶肽。其一级结构是通过固相埃德曼降解和质谱联用获得的。胰蛋白酶肽的大部分似乎不受蛋白水解酶作用的影响。该肽跨越了约勒斯等人（《生物化学与生物物理研究通讯》（1979年）87卷，619 - 626页）在完整蛋白质的COOH末端区域定位的三个溴化氰肽。该区域的二级结构计算表明可分为离散结构域，大部分胰蛋白酶肽对应一个高度有序的疏水性结构域；预测该区域形成α螺旋或β结构的概率相等。
