Richman J B, Verpoorte J A
Can J Biochem. 1981 Jul;59(7):519-23. doi: 10.1139/o81-072.
The alpha 2-macroglobulin (alpha 2-M) was purified from the plasma of normal individuals and from that of cystic fibrosis patients. The proteins exhibited identical optical properties. Both proteins have an absorbance coefficient of A = 1060 g . cm-2 at 280 nm. The circular dichroism spectra are identical and indicate about 45% beta-sheet structure and almost no alpha-helix. The spectra of solutions at pH 8.0 do not change when trypsin is added. The fluorescence spectra of the alpha 2-M measured at pH 8.0 have contributions by tyrosine and tryptophan residues. The fluorescence intensities are identical and are enhanced about 30% when trypsin is added in 2:1 molar ratios.
从正常个体和囊性纤维化患者的血浆中纯化出α2-巨球蛋白(α2-M)。这些蛋白质表现出相同的光学性质。两种蛋白质在280nm处的吸光系数均为A = 1060 g·cm-2。圆二色光谱相同,表明约45%为β-折叠结构,几乎没有α-螺旋。当加入胰蛋白酶时,pH 8.0溶液的光谱不变。在pH 8.0下测量的α2-M的荧光光谱有酪氨酸和色氨酸残基的贡献。荧光强度相同,当以2:1的摩尔比加入胰蛋白酶时,荧光强度增强约30%。