Gordon C N
Adv Exp Med Biol. 1977;86A:649-56. doi: 10.1007/978-1-4684-3282-4_39.
Oligomeric proteins can be intramolecularly cross-linked with polylysine in a reaction in which a water soluble carbodiimide mediates an amide linkage between the protein carboxyl groups and the epsilon-amino groups of polylysine. Studies carried out with a cytochrome p-450 indicate that a small number of molecules in a population which has been cross-linked in this way retain important features of their tertiary and quaternary structure when negatively stained and examined in the electron microscope. Use of the method in determining the subunit geometry of oligomeric proteins is discussed.
寡聚蛋白可在一种反应中与聚赖氨酸进行分子内交联，在此反应中，水溶性碳二亚胺介导蛋白质羧基与聚赖氨酸的ε-氨基之间形成酰胺键。对细胞色素P-450进行的研究表明，以这种方式交联的群体中的少数分子在负染色并在电子显微镜下检查时保留了其三级和四级结构的重要特征。本文讨论了该方法在确定寡聚蛋白亚基几何结构中的应用。
