Liepnieks J J, Dwulet F E, Benson M D
Department of Medicine, Indiana University School of Medicine, Indianapolis.
Mol Immunol. 1990 Jun;27(6):481-5. doi: 10.1016/0161-5890(90)90066-9.
The complete amino acid sequence of amyloid protein AND is presented. Amyloid fibrils were isolated from the spleen of patient AND, and the subunit protein was isolated from the fibrils after reduction and carboxymethylation. Sequence analysis of intact protein AND identified it as a kappa I immunoglobulin light chain. The complete sequence was determined from its tryptic peptides. The protein contained the entire variable region and the constant region to position 145 of the light chain. Several unique amino acid substitutions were found in protein AND compared to other kappa I proteins. The glycine, serine, arginine, threonine, alanine and arginine at positions 31, 45, 55, 76, 85 and 107, respectively, are reported for the first time in a kappa I protein. A number of uncommon amino acid substitutions were found in the framework regions in protein AND around the contact region of the dimer which may result in the molecule becoming more susceptible to fibril formation.
本文展示了淀粉样蛋白AND的完整氨基酸序列。淀粉样纤维从患者AND的脾脏中分离得到,亚基蛋白在还原和羧甲基化后从纤维中分离出来。完整蛋白AND的序列分析确定其为κI免疫球蛋白轻链。通过胰蛋白酶肽段确定了完整序列。该蛋白包含轻链的整个可变区和至第145位的恒定区。与其他κI蛋白相比,在蛋白AND中发现了几个独特的氨基酸取代。分别位于第31、45、55、76、85和107位的甘氨酸、丝氨酸、精氨酸、苏氨酸、丙氨酸和精氨酸在κI蛋白中首次报道。在蛋白AND的二聚体接触区域周围的框架区域中发现了许多不常见的氨基酸取代,这可能导致该分子更容易形成纤维。