RAMAN AND FOURIER-TRANSFORM INFRARED SPECTROSCOPIC STUDIES OF THE INTERACTION BETWEEN GLYCOPHORIN AND DIMYRISTOYLPHOSPHATIDYLCHOLINE

被引：62

作者：

MENDELSOHN, R ^{[1
]}

DLUHY, R ^{[1
]}

TARASCHI, T ^{[1
]}

CAMERON, DG ^{[1
]}

MANTSCH, HH ^{[1
]}

机构：

[1] NATL RES COUNCIL CANADA, DIV CHEM, OTTAWA K1A 0R6, ONTARIO, CANADA

来源：

BIOCHEMISTRY | 1981年 / 20卷 / 23期

关键词：

D O I：

10.1021/bi00526a027

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

Glycophorin from the human erythrocyte membrane has been isolated in pure form and reconstituted into large unilamellar vesicles with 1,2-dimyristoyl-3-sn-phosphatidylcholine at lipid/protein mole ratios ranging from 50:1-200:1. The effect of protein on the phospholipid phase transition was monitored by Raman and Fourier transform IR spectroscopy and differential scanning calorimetry. No evidence for an immobilized higher melting lipid component is observed. The gel to liquid-crystalline phase transition is significantly broadened and shifted to lower temperatures as the proportion of protein is increased, while the pretransition is abolished. At all temperatures, the mobility of the acyl chains is increased by the addition of protein while interchain lateral interactions are disrupted. There is no evidence for a significant change in the conformational order at low temperatures (.apprx. 5.degree. C) or in the liquid-crystalline phase.

引用

页码：6699 / 6706

页数：8

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