Toft K G, Sletten K, Husby G
Biol Chem Hoppe Seyler. 1985 Jul;366(7):617-25. doi: 10.1515/bchm3.1985.366.2.617.
The amino-acid sequence of the variable region of a carbohydrate-containing amyloid fibril protein EPS of immunoglobulin lambda light chain origin has been elucidated. The protein was isolated from the liver of a patient (EPS) with an immunocyte dyscrasia of the IgM type. The molecular mass of this protein was found to be about 20 kDa including an oligosaccharide chain linked to it. The amino-acid sequence determination involved automatic Edman degradation of polypeptides obtained after cleaving the protein with BNPS-skatole, trypsin and thermolysin. The proposed sequence of the variable region of the protein showed that it may be assigned to the V lambda I subgroup. A tryptic and a thermolysinolytic peptide both containing the carbohydrate were isolated and characterized, and the localization of an oligosaccharide chain linked to asparagine was established.
已阐明源自免疫球蛋白λ轻链的含碳水化合物淀粉样原纤维蛋白EPS可变区的氨基酸序列。该蛋白是从一名患有IgM型免疫细胞发育异常的患者(EPS)的肝脏中分离出来的。发现该蛋白的分子量约为20 kDa,包括与之相连的一条寡糖链。氨基酸序列测定涉及用BNPS-粪臭素、胰蛋白酶和嗜热菌蛋白酶切割该蛋白后获得的多肽的自动Edman降解。该蛋白可变区的推测序列表明它可能属于VλI亚组。分离并鉴定了两条均含有碳水化合物的胰蛋白酶肽和嗜热菌蛋白酶肽,并确定了与天冬酰胺相连的寡糖链的定位。