Jones A J, Rumsby M G
Biochem J. 1977 Dec 1;167(3):583-91. doi: 10.1042/bj1670583.
The myelin basic protein from bovine brain tissue was purified and the two peptides obtained by cleavage of the polypeptide chain at the single tryptophan residue were isolated. The interaction of these peptides and the intact basic protein with complex lipids was investigated by following the solubilization of lipid-protein complexes into chloroform in a biphasic solvent system. The C-terminal peptide fragment (residues 117-170) and the intact basic protein both formed chloroform-soluble complexes with acidic lipids, but not with neutral complex lipids. The N-terminal fragment (residues 1-115) did not form chloroform-soluble complexes with either acidic or neutral complex lipids. The molar ratio of lipid to protein that caused a 50% loss of protein from the upper phase to the lower chloroform phase was the same for the intact basic protein as for the smaller C-terminal peptide fragment. Phosphatidylserine and phosphatidylinositol were approximately twice as efficient as sulphatide at causing protein redistribution to the chloroform phase. The results are interpreted as indicating that the sites for ionic interactions between lipid and charged groups on the basic protein of myelin are located in the C-terminal region of the protein molecule.
从牛脑组织中纯化出髓鞘碱性蛋白，并分离出通过在单个色氨酸残基处切割多肽链而获得的两种肽。通过在双相溶剂系统中跟踪脂质 - 蛋白质复合物溶解到氯仿中的情况，研究了这些肽以及完整碱性蛋白与复合脂质的相互作用。C末端肽片段（第117 - 170位氨基酸残基）和完整碱性蛋白都与酸性脂质形成了氯仿可溶的复合物，但与中性复合脂质则未形成。N末端片段（第1 - 115位氨基酸残基）与酸性或中性复合脂质均未形成氯仿可溶的复合物。导致50%的蛋白质从上层相转移到下层氯仿相的脂质与蛋白质的摩尔比，对于完整碱性蛋白和较小的C末端肽片段来说是相同的。磷脂酰丝氨酸和磷脂酰肌醇在促使蛋白质重新分布到氯仿相方面的效率约为硫脂的两倍。这些结果被解释为表明髓鞘碱性蛋白上脂质与带电基团之间的离子相互作用位点位于蛋白质分子的C末端区域。
