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波罗蜜凝集素与人类IgA的相互作用不涉及免疫球蛋白的天冬酰胺连接的寡糖。

Interaction of Artocarpus lectins with human IgA does not involve asparagine-linked oligosaccharide of the immunoglobulin.

作者信息

Hashim O H, Kobayashi K, Taniguchi N

机构信息

Department of Biochemistry, Faculty of Medicine, University of Malaya, Kuala Lumpur.

出版信息

Biochem Int. 1992 Jul;27(3):423-9.

PMID:1417879
Abstract

In view of the controversy with respect to the interaction of jacalin with human IgA2, a study was undertaken to assess the reactivity of the Artocarpus heterophyllus lectin, as well as the lectin from Artocarpus integer (lectin C), with subclasses of human immunoglobulin A by ELISA. Our data is consistent with the view that Artocarpus lectins have no affinity for the IgA2 immunoglobulins. In further support of the findings, we have established that N-linked oligosaccharide moieties of IgA have no significant bearing in the lectin-immunoglobulin binding. Interaction was also not affected in the presence of 1% (w/v) BSA.

摘要

鉴于关于jacalin与人类IgA2相互作用存在争议,开展了一项研究,通过酶联免疫吸附测定法评估面包果凝集素以及尖叶桂木凝集素(凝集素C)与人类免疫球蛋白A亚类的反应性。我们的数据与面包果凝集素对IgA2免疫球蛋白无亲和力这一观点一致。为进一步支持这些发现,我们已确定IgA的N-连接寡糖部分在凝集素-免疫球蛋白结合中无显著影响。在存在1%(w/v)牛血清白蛋白的情况下,相互作用也未受影响。

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