Mitchell T J, Reilly T M
E.I. du Pont de Nemours and Company, Medical Products Department, Wilmington, DE 19880-0400.
Pept Res. 1990 Nov-Dec;3(6):277-81.
To relate the immunochemical specificity of three murine monoclonal antibodies directed against the octapeptide hormone angiotensin II (AII) to their primary structure, we have sequenced mRNA for the variable regions of their heavy and light chains. Comparison of the sequences indicates that each of the antibodies utilize very closely related V genes in both heavy and light chains. Two of these antibodies, ICH2 and ICA10, display an epitope preference for the carboxy terminus of AII. A third monoclonal antibody, KAA8, displays a lesser specificity for the carboxy terminus of AII than either ICH2 or ICA10. This antibody differs in sequence from the others mainly in the light chain complementarity determining regions (CDR) 1 and 3 and in CDR 3 (D region) on the heavy chain. We interpret these sequence differences as the basis for the observed specificity preferences.
为了将三种针对八肽激素血管紧张素II（AII）的鼠单克隆抗体的免疫化学特异性与其一级结构相关联，我们对其重链和轻链可变区的mRNA进行了测序。序列比较表明，每种抗体在重链和轻链中都利用了非常密切相关的V基因。其中两种抗体，ICH2和ICA10，对AII的羧基末端表现出表位偏好。第三种单克隆抗体KAA8对AII羧基末端的特异性低于ICH2或ICA10。该抗体与其他抗体的序列差异主要在于轻链互补决定区（CDR）1和3以及重链上的CDR 3（D区）。我们将这些序列差异解释为观察到的特异性偏好的基础。
