Rivat C, Schiff C, Rivat L, Ropartz C, Fougereau M
Eur J Immunol. 1976 Aug;6(8):545-51. doi: 10.1002/eji.1830060804.
In this paper we report the structural basis for the nonexpression of G1m(3) and Km (1,2) allotypes in an IgG1 (kappa) human myeloma protein (protein LEC). Heavy and light chains spontaneously dissociate in sodium dodecyl sulfate polyacrylamide gels. Light chains appear to be covalently S-S bonded. Analysis of cysteine-containing peptides shows that the heavy chain of the IgG protein LEC has a deletion of residues 216-230, thus encompassing the entire hinge region. An arginine residue, characteristic of the G1m(3) marker is present at position 214. An alanine at position 153 and a leucine at position 191 of the light chain, characteristic of the Km (1, 2) allotypes, are present. It is likely that the double Km and Gm lack of expression is the result of the deletion. The genetic implications of the sequence of this protein are discussed.
在本文中,我们报告了在一种IgG1(κ)人骨髓瘤蛋白(蛋白LEC)中G1m(3)和Km(1,2)同种异型不表达的结构基础。重链和轻链在十二烷基硫酸钠聚丙烯酰胺凝胶中自发解离。轻链似乎通过共价二硫键连接。对含半胱氨酸肽段的分析表明,IgG蛋白LEC的重链缺失了216 - 230位残基,从而涵盖了整个铰链区。在214位存在一个精氨酸残基,这是G1m(3)标记的特征。轻链的153位是丙氨酸,191位是亮氨酸,这是Km(1,2)同种异型的特征。双Km和Gm缺乏表达很可能是缺失的结果。本文还讨论了该蛋白序列的遗传学意义。