Schwenke K D, Staatz A, Mothes R, Seifert A, Dautzenberg H
WIP-Research Group in Plant Protein Chemistry, University of Potsdam, Germany.
Int J Pept Protein Res. 1996 Apr;47(4):254-9. doi: 10.1111/j.1399-3011.1996.tb01353.x.
Legumin-T, the high-molecular mass product of limited tryptic hydrolysis of faba bean legumin, was investigated using hydrodynamic methods, static light scattering, fluorescence and ultraviolet spectroscopy. The following physico-chemical parameters were determined in a high-ionic strength buffer system: molecular mass, 2.4 x 10(5) g/mol; sedimentation coefficient, SO20 = 10.8 x 10(-13)Si; diffusion coefficient, DO20 = 4.1 x 10(-7) cm2 s-1; intrinsic viscosity, [eta] = 3.51 mL/g; partial specific volume, v = 0.719 mL/g; frictional ratio, f/f0 = 1.22; shape factor, beta = 2.17 x 10(6). Conformational changes during the formation of legumin-T can be deduced from the fluorescence emission and UV spectra.
使用流体动力学方法、静态光散射、荧光和紫外光谱对蚕豆球蛋白经有限胰蛋白酶水解得到的高分子量产物Legumin-T进行了研究。在高离子强度缓冲系统中测定了以下物理化学参数：分子量为2.4×10⁵ g/mol；沉降系数，S₂₀ = 10.8×10⁻¹³ S；扩散系数，D₂₀ = 4.1×10⁻⁷ cm² s⁻¹；特性粘度，[η] = 3.51 mL/g；比容，v = 0.719 mL/g；摩擦比，f/f₀ = 1.22；形状因子，β = 2.17×10⁶。从荧光发射和紫外光谱可以推断出Legumin-T形成过程中的构象变化。
