Binding capacity of alpha-crystallin to bovine lens lipids
Binding capacity of alpha-crystallin to bovine lens lipids
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DOI：
10.1006/exer.1996.0130
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发表时间：
1996-10-01
影响因子：
3.4
通讯作者：
Tang, DX
中科院分区：
文献类型：
--
作者：
Borchman, D;Tang, DX
通过三个实验来测定牛晶状体脂质囊泡的α -结晶蛋白结合能力。在一个实验中，脂质保持不变（2.5 mg ml(-1)）， α -结晶蛋白浓度改变（0.5 ~ 3.0 mg ml(-1)）。在另一个实验中，α -晶体蛋白保持不变（1 mg ml(-1)），脂质浓度变化（0.25 ~ 3 mg ml(-1)）。我们计算出脂质的结合能力为0.33 +/-0.05 (S.D.) mg α -晶体蛋白（mg晶状体脂质）（-1）。在0.33 mg α -晶体蛋白（mg透镜脂）（-1）附近，探针的荧光强度和各向异性增加并趋于稳定，这表明随着α -晶体蛋白的结合，水被排除在双分子层的头组区域之外，头组区域变得不那么可移动。α -结晶蛋白结合可能具有保护和稳定脂质双分子层，降低膜通透性的作用。(C) 1996学术出版社有限公司
Three experiments were performed to determine the alpha-crystallin binding capacity of bovine lens lipid vesicles. In one experiment lipid was kept constant (2.5 mg ml(-1)) and the alpha-crystallin concentration was changed (0.5 to 3.0 mg ml(-1)). In another experiment, alpha-crystallin was kept constant (1 mg ml(-1)) and the concentration of lipid was varied (0.25 to 3 mg ml(-1)). We calculated the binding capacity of the lipid to be 0.33 +/-0.05 (S.D.) mg alpha-crystallin (mg lens lipid)(-1). This was confirmed by changes in the anisotropy and fluorescent intensity of a probe that partitions at the headgroup region of the lipid bilayer, Near 0.33 mg alpha-crystallin (mg lens lipid)(-1) the fluorescence intensity and anisotropy of the probe increases and plateaus which indicates that concomitant with alpha-crystallin binding, water is excluded from the head group region of the bilayer and the headgroup region becomes less mobile. It is possible that alpha-crystallin binding could protect and stabilize the lipid bilayer and decrease membrane permeability. (C) 1996 Academic Press Limited