Alcaraz G, Bourgois A, Moulin A, Bazin H, Fougereau M
Ann Immunol (Paris). 1980 May-Jun;131C(3):363-88.
The isolation, purification and characterization of the rat IR-731 monoclonal immunoglobulin is reported. The molecule is IgD-like, as appreciated from immunochemical and biochemical characteristics. H and L chains, Fab and Fc tryptic fragments have been isolated, analyzed, and partial sequence data have been obtained, including most cysteyl-containing peptides. The heavy chain contains a deletion which encompasses most of the CH2 domain and the beginning of the CH2 domain, and observation which does not reflect the intron-exon organization depicted for some murine heavy chains at the gene level. Basic structural features of the hinge region of the IgD molecule (extreme susceptibility to proteolytic enzymes, presence of basic amino acids near its COOH-terminus) have been found for the IR-731 molecule. In addition, partial sequence of the light chains points to the existence of K subgroups in the rat. Very limited amino acid changes have been identified in the K constant region, suggesting a possible--but limited--polymorphism which might be isotypic and/or allotypic in nature.
本文报道了大鼠IR-731单克隆免疫球蛋白的分离、纯化及特性鉴定。从免疫化学和生化特性来看，该分子类似IgD。已分离、分析了重链和轻链、Fab和Fc胰蛋白酶片段，并获得了部分序列数据，包括大多数含半胱氨酸的肽段。重链存在一个缺失，该缺失涵盖了大部分CH2结构域和CH3结构域的起始部分，这一观察结果与基因水平上某些小鼠重链所描述的内含子-外显子组织情况不符。在IR-731分子中发现了IgD分子铰链区的基本结构特征（对蛋白水解酶极度敏感，在其COOH末端附近存在碱性氨基酸）。此外，轻链的部分序列表明大鼠中存在K亚群。在K恒定区已鉴定出非常有限的氨基酸变化，这表明可能存在一种性质上可能是同种型和/或异型的、但有限的多态性。
