PHASE SEPARATION OF ACIDIC AND NEUTRAL PHOSPHOLIPIDS INDUCED BY HUMAN MYELIN BASIC-PROTEIN
PHASE SEPARATION OF ACIDIC AND NEUTRAL PHOSPHOLIPIDS INDUCED BY HUMAN MYELIN BASIC-PROTEIN
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DOI:
10.1021/bi00644a003
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发表时间:
1977-01-01
期刊:
影响因子:
2.9
通讯作者:
PAPAHADJOPOULOS, D
中科院分区:
文献类型:
--
作者:
BOGGS, JM;MOSCARELLO, MA;PAPAHADJOPOULOS, D
Differential scanning calorimetry was used to detect lipid phase separation induced in mixtures of acidic and neutral phospholipids by myelin basic protein from human CNS myelin. Phosphatidic acid, phosphatidylglycerol and phosphatidylserine mixtures with phosphatidylcholine (PC) were used and were nearly randomly mixed in the absence of the protein. Incorporation of basic protein into these mixtures caused a shift in the phase transition temperature toward the temperature of the PC component, indicating that it binds and separates out the acidic lipid leaving a PC-enriched phase. In some cases a transition due to the acidic lipid-basic protein complex was also observed. The shift towards the transition temperature of the PC component occurred regardless of whether the PC was the lower melting or the higher melting component of the mixture. The protein did not just bind to the lipid which melts first, but bound to the acidic lipid even if it melts at a much higher temperature than the neutral lipid. If enough acidic lipid was available, the protein could bind to 27-34 molecules of acidic lipid per molecule of protein. At pH 7.4 basic protein has 38 basic residues; thus, nearly all of these can be involved in electrostatic binding to acidic lipid polar head groups resulting in lipid phase separation.