Scholz R, Hilschmann N
Hoppe Seylers Z Physiol Chem. 1975 Aug;356(8):1333-5.
The primary structure of a monoclonal human IgA immunoglobulin has been determined. The protein has been isolated from the serum by salt fractionation, ion exchange chromatography and gel filtration. The L-chain was isolated by gel filtration after partial reduction and alkylation of the IgA-molecule. The primary structure of the L-chain was determined by sequence studies of its tryptic peptides. The protein containes 216 amino acid residues. Based on its homology with other proteins of known structure, the variable part of the protein clearly belongs to subgroup II of the lambda-chains. The constant part of the chain is Kern- and Oz-, which means that it has serine in position 154 and arginine in position 191.
已确定一种单克隆人IgA免疫球蛋白的一级结构。该蛋白质通过盐析、离子交换色谱和凝胶过滤从血清中分离出来。L链是在IgA分子部分还原和烷基化后通过凝胶过滤分离得到的。L链的一级结构通过对其胰蛋白酶肽段的序列研究来确定。该蛋白质含有216个氨基酸残基。基于其与其他已知结构蛋白质的同源性,该蛋白质的可变部分明显属于λ链的II亚组。该链的恒定部分是Kern-和Oz-型,这意味着它在第154位有丝氨酸,在第191位有精氨酸。