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EFFECT OF FATTY ACYL CHAIN-LENGTH OF PHOSPHATIDYLCHOLINE ON THEIR TRANSFER FROM LIPOSOMES TO ERYTHROCYTES AND TRANSVERSE DIFFUSION IN THE MEMBRANES INFERRED BY TEMPO-PHOSPHATIDYLCHOLINE SPIN PROBES
被引:17
|作者:
TAMURA, A
YOSHIKAWA, K
FUJII, T
OHKI, K
NOZAWA, Y
SUMIDA, Y
机构:
[1] KYOTO PHARMACEUT UNIV, DEPT BIOCHEM, YAMASHINA KU, KYOTO 607, JAPAN
[2] KYOTO PHARMACEUT UNIV, DEPT PHARMACEUT CHEM, YAMASHINA KU, KYOTO 607, JAPAN
[3] GIFU UNIV, SCH MED, DEPT BIOCHEM, GIFU 500, JAPAN
关键词:
D O I:
10.1016/0005-2736(86)90171-9
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:
TEMPO-phosphatidylcholine (PC) spin probes which have homologous saturated acyl chains of 10, 12, 14 and 16 carbon atoms, were synthesized as analogues of PC. Transfer of TEMPO-PCs from liposomal membrane to the ghost membrane of human erythrocyte and transverse diffusion of TEMPO-PCs within the membrane of intact erythrocytes were determined by measurement of spontaneous increase and decrease in signal amplitude of an anisotropic triplet spectrum, due to dilution of the label by natural phospholipid of the membrane and reduction of the label by the cytoplasmic content of the erythrocyte, respectively. TEMPO-PC molecules in TEMPO-PC liposomes, except dipalmitoyl TEMPO-PC, were rapidly incorporated into the ghost membrane by incubation at 37.degree. C; the PC having shorter acyl chains was transferred faster. The cytoplasmic content of the erythrocyte rapidly reduced the nitroxide radical of the spin probe. The central peak height of ESR signal was once increased by incorporation of TEMPO-PC into the erythrocyte membrane and then was spontaneously decreased during further incubation at 37.degree. C. This decrease indicates that PC molecules traverse from the outer to the inner layer of the membrane lipid bilayer. The decrease of signal amplitude was faster with PC of shorter acyl chain. These findings suggest that both transfer between membranes and transverse diffusion in the membrane may be favored to the PC species with shorter acyl chains.
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页码:250 / 256
页数:7
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