Streefkerk D G, Glaudemans C P
Biochemistry. 1977 Aug 23;16(17):3760-5. doi: 10.1021/bi00636a005.
Four murine myeloma immunoglobulins, A4, A47N, U61, and E109, have been studied for their binding affinities with inulin and a series of oligosaccharides derived from inulin. The results indicate that the combining site of these immunoglobulins shows highest complementarity for a trifructofuranosyl sequence (A4 and A47N) and a tetrafructofuranosyl sequence (U61 and E109). The size of the combining area of the immunoglobulin E109 derived from the antigenic determinant (approximately 15 X 14 X 10 A) agrees well with the size observed on a hypothetical space model of the Fv portion of E109 (Potter, M., Rudikoff, S., Padlan, E. A., and Vrana, M. (1976), Antibodies in Human Diagnosis and Therapy, Haber, E., and Krause, R.M., Ed., New York, N.Y., Raven Press).
已对四种鼠源骨髓瘤免疫球蛋白A4、A47N、U61和E109与菊粉及一系列菊粉衍生寡糖的结合亲和力进行了研究。结果表明,这些免疫球蛋白的结合位点对三呋喃果糖基序列(A4和A47N)和四呋喃果糖基序列(U61和E109)表现出最高的互补性。源自抗原决定簇的免疫球蛋白E109结合区域的大小(约15×14×10埃)与在E109 Fv部分的假设空间模型上观察到的大小非常吻合(波特,M.,鲁迪科夫,S.,帕德兰,E.A.,和弗拉纳,M.(1976年),《人类诊断和治疗中的抗体》,哈伯,E.,和克劳斯,R.M.编,纽约,纽约州,拉文出版社)。