Schwenke K D, Zirwer D, Gast K, Görnitz E, Linow K J, Gueguen J
Zentralinstitut für Ernährung, Potsdam-Rehbrücke, Federal Republic of Germany.
Eur J Biochem. 1990 Dec 12;194(2):621-7. doi: 10.1111/j.1432-1033.1990.tb15661.x.
The influence of various levels of succinylation on the structure of the legumin from pea seed has been studied by the techniques of sedimentation velocity, viscometry, fluorescence and circular dichroism spectroscopy, as well as dynamic light scattering. The protein dissociates gradually into the 3S subunit forming a 7S intermediate. At a level of 75-80% succinylation, sudden unfolding of the protein occurs characterized by drastic changes in viscometric and spectroscopic properties. The fluorescence spectra point to the formation of a novel organized structure at a moderate degree of modification before the molecular unfolding takes place. The succinylated subunit was shown to have a sedimentation coefficient of 3.2S, a diffusion coefficient of 5.03 x 10(-7) cm2 . s-1 a Stokes' radius of 4.24 nm, a partial specific volume of 0.703 ml/g, an intrinsic viscosity of 0.13 dl/g, a molar mass of 52.2 kDa and a frictional ratio of 1.74.
通过沉降速度、粘度测定、荧光和圆二色光谱以及动态光散射技术，研究了不同琥珀酰化水平对豌豆种子豆球蛋白结构的影响。该蛋白质逐渐解离成3S亚基，形成7S中间体。在琥珀酰化水平为75-80%时，蛋白质会突然展开，其特征是粘度和光谱性质发生剧烈变化。荧光光谱表明，在分子展开之前，适度修饰程度下会形成一种新型有序结构。琥珀酰化亚基的沉降系数为3.2S，扩散系数为5.03×10(-7) cm2·s-1，斯托克斯半径为4.24 nm，偏比容为0.703 ml/g，特性粘度为0.13 dl/g，摩尔质量为52.2 kDa，摩擦比为1.74。
