Fu L, Liang J J
Center for Ophthalmic Research, Brigham and Women's Hospital, Department of Ophthalmology, Harvard Medical School, Boston, MA 02115, USA.
Mol Vis. 2001 Jul 26;7:178-83.
To compare the spectroscopic and unfolding properties of human lens [beta]B2- and [gamma]C-crystallin with those of [alpha]A-crystallin.
Human lens [beta]B2- and [gamma]C-crystallin were cloned and measured spectroscopically. The unfolding curves in response to guanidine HCl (GdnHCl) and heat were also obtained by measuring Trp fluorescence emission intensity or emission maximum wavelength with increasing perturbation.
Very similar spectroscopic and unfolding properties were seen with [beta]B2- and [gamma]C-crystallin, but both demonstrated great differences compared with [alpha]A-crystallin. Unlike [alpha]A-crystallin, [beta]B2- and [gamma]C-crystallin showed very little binding to Bis-ANS (4,4'-dianilino-1,1'-binaphthalene-5,5'-disulfonic acid), a hydrophobic fluorescence probe. Both [beta]B2- and [gamma]C-crystallin were more resistant than [alpha]A-crystallin to GdnHCl-induced unfolding, but [alpha]A-crystallin was more resistant than [beta]B2- and [gamma]C-crystallin to heat induced unfolding.
It was observed that [beta]B2- and [gamma]C-crystallin showed more similar spectroscopic and unfolding properties with each other than each of them showed with [alpha]A-crystallin.
比较人晶状体βB2-和γC-晶状体蛋白与αA-晶状体蛋白的光谱特性和去折叠特性。
克隆人晶状体βB2-和γC-晶状体蛋白并进行光谱测量。通过随着胍盐酸盐（GdnHCl）和热扰动增加测量色氨酸荧光发射强度或发射最大波长，也获得了响应于GdnHCl和热的去折叠曲线。
βB2-和γC-晶状体蛋白具有非常相似的光谱特性和去折叠特性，但与αA-晶状体蛋白相比两者均表现出很大差异。与αA-晶状体蛋白不同，βB2-和γC-晶状体蛋白与疏水荧光探针双-ANS（4,4'-二苯胺基-1,1'-联萘-5,5'-二磺酸）的结合非常少。βB2-和γC-晶状体蛋白比αA-晶状体蛋白对GdnHCl诱导的去折叠更具抗性，但αA-晶状体蛋白比βB2-和γC-晶状体蛋白对热诱导的去折叠更具抗性。
观察到βB2-和γC-晶状体蛋白彼此之间的光谱特性和去折叠特性比它们与αA-晶状体蛋白的光谱特性和去折叠特性更相似。
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