Douglas Borchman, Daxin Tang, Marta C. Yappert
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引用次数: 83
Abstract
Membrane lipid composition varies in different tissues and species. Since a defined lipid composition is essential to the function of many membranes, the relationship between membrane lipid composition and structure was determined using infrared and Raman spectroscopy in four membranes containing a calcium pump: rabbit fast and slow twitch muscle sarcoplasmic reticulum and human and bovine lens fiber cell membranes. We found that membrane sphingolipid and phosphatidylcholine content were correlated to a decrease and increase, respectively, in the infrared lipid CH2 symmetric stretching band frequency. We interpret the change in frequency as a change in lipid hydrocarbon chain structural order. This was confirmed by Raman order parameters. The high degree of hydrocarbon chain saturation found in the variable amide chains of sphingolipids is likely to account for this correlation. Lipid phase transition temperature and cooperativity also correlated to sphingolipid and phosphatidylcholine content, and are the forces defining the order in at physiological temperature in the samples studied. Ca2+-ATPase caused an increase in the CH2 symmetric stretching frequency in fast twitch muscle sarcoplasmic reticulum (interpreted as an increase in hydrocarbon chain disorder), but had no effect on slow twitch muscle sarcoplasmic reticulum lipid hydrocarbon chain structure. In the natural systems studied, we find that it is the lipid hydrocarbon chain saturation that defines lipid hydrocarbon chain order. © 1999 John Wiley & Sons, Inc. Biospectroscopy 5: 151–167, 1999
晶状体和肌浆网膜的脂质组成、膜结构关系
膜脂组成在不同的组织和物种中是不同的。由于确定的脂质组成对许多膜的功能至关重要,因此使用红外和拉曼光谱确定了含钙泵的四种膜的膜脂组成与结构之间的关系:兔快、慢抽搐肌肌浆网和人和牛晶态纤维细胞膜。我们发现膜鞘脂和磷脂酰胆碱含量分别与红外脂质CH2对称拉伸带频率的降低和增加相关。我们将频率的变化解释为脂质烃链结构顺序的变化。拉曼序参数证实了这一点。在鞘脂的可变酰胺链中发现的高度烃链饱和可能解释了这种相关性。脂质相变温度和协同性也与鞘脂和磷脂酰胆碱含量相关,是确定所研究样品在生理温度下的顺序的力。Ca2+- atp酶引起快抽动肌肌浆网CH2对称拉伸频率增加(解释为碳氢链紊乱增加),但对慢抽动肌肌浆网脂质碳氢链结构无影响。在研究的自然系统中,我们发现脂质烃链的饱和度决定了脂质烃链的顺序。©1999 John Wiley &儿子,Inc。生物光谱学学报(自然科学版),1999
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