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免疫球蛋白G分子的柔性结构。使用芳基萘磺酸盐作为配体对半抗原-抗半抗原抗体相互作用进行的荧光去极化研究。

Flexible structure of immunoglobulin G molecule. Fluorescence depolarization studies on hapten-antihapten antibody interactions using arylnaphthalenesulfonates as the ligands.

作者信息

Murakami K, Nakamura H

出版信息

Jpn J Exp Med. 1976 Feb;46(1):59-70.

PMID:945389
Abstract

Fluorescence depolarization studies on immunoglobulin G, Fab'2 and Fab' fragments were carried out using isomeric anilinonaphthalenesulfonates and their corresponding rabbit antibody systems, and the values of the relaxation time rho(h) were calculated. From the results it was confirmed that the IgG and Fab'2 fragment have a certain degree of segmental flexibility, and suggested that these divalent antibody molecules have the same order of flexibilities. Furthermore, the rhoh values of the Fab' fragments from each antibody preparation were also determined and conflicting results were obtained with the samples from two different kinds of antibody systems against the isomeric ligands. The results were discussed with special references to the orientation of ligands bound to the antibody combining sites.

摘要

使用异构苯胺基萘磺酸盐及其相应的兔抗体系统对免疫球蛋白G、Fab'2和Fab'片段进行了荧光去极化研究,并计算了弛豫时间rho(h)的值。结果证实IgG和Fab'2片段具有一定程度的片段灵活性,并表明这些二价抗体分子具有相同的灵活性顺序。此外,还测定了每种抗体制备物中Fab'片段的rhoh值,并且针对异构配体的两种不同抗体系统的样品得到了相互矛盾的结果。结合与抗体结合位点结合的配体的取向对结果进行了讨论。

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