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循环激活表位结合分子对抗体介导的缺陷性β-D-半乳糖苷酶激活的特异性抑制作用。

Specific inhibition of the antibody-mediated activation of a defective beta-D-galactosidase by circulating activating epitope-binding molecules.

作者信息

Conway de Macario E, Macario A J

出版信息

J Immunol. 1979 Jul;123(1):442-6.

PMID:87481
Abstract

Activation of a defective Escherichia coli beta-D-galactosidase by specific activating antibody is inhibited competitively by a molecule with immunoglobulin properties but devoid of activating capacity. This molecule is found in the serum of nonimmunized rabbits and is no longer detectable after beta-D-galactosidase administration, but can be demonstrated in rabbits injected with antigens other than the enzyme. The data show that the inhibitory molecule recognizes and interacts specifically with the activating epitope of the activatable enzyme and that, although unable to activate the latter, it competes with the activating antibody and inhibits activation.

摘要

具有免疫球蛋白特性但缺乏激活能力的分子可竞争性抑制特异性激活抗体对缺陷型大肠杆菌β-D-半乳糖苷酶的激活作用。这种分子存在于未免疫兔子的血清中,在给予β-D-半乳糖苷酶后就无法再检测到,但在注射该酶以外抗原的兔子中可以检测到。数据表明,抑制性分子可识别可激活酶的激活表位并与之特异性相互作用,并且尽管其无法激活后者,但它可与激活抗体竞争并抑制激活作用。

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