抗MLI单克隆抗体与欧洲槲寄生凝集素同工型的相互作用。

The interactions of anti-MLI monoclonal antibodies with isoforms of the lectin from Viscum album.

作者信息

Tonevitsky A G, Rakhmanova V A, Agapov I I, Shamshiev A T, Usacheva E A, Prokoph'ev S A, Denisenko O N, Pfueller U

机构信息

State Scientific Center of Russian Federation Gniigenetika, Moscow.

出版信息

Immunol Lett. 1995 Jan;44(1):31-4. doi: 10.1016/0165-2478(94)00181-p.

DOI:10.1016/0165-2478(94)00181-p

PMID:7721340

Abstract

Monoclonal antibodies (mAb) reacting with native (TA5, TB12) and denatured (T33, T35) plant toxin mistletoe lectin I (MLI) from Viscum album have been obtained. The interaction between mAbs and native toxin with ML isoforms (MLII, MLIII) has been investigated. An immunological cross-reaction has been shown to take place for mAb TA5 (anti-A-chain of MLI) between MLII and MLIII isoforms of toxin. TA5 has not inhibited enzyme activity of the A-chain in a rabbit reticulocyte cell-free system. TB12 has been shown to react with the galactose-binding site of the B-chain. TA5 and TB12 have shown no cross-reaction with plant toxin ricin. The association constants for mAbs have been determined. The nature of heterogeneity of the lectins from Viscum album is discussed.

摘要

已获得与来自欧洲槲寄生的天然（TA5、TB12）和变性（T33、T35）植物毒素槲寄生凝集素I（MLI）发生反应的单克隆抗体（mAb）。研究了单克隆抗体与天然毒素以及ML同工型（MLII、MLIII）之间的相互作用。已证明单克隆抗体TA5（抗MLI A链）在毒素的MLII和MLIII同工型之间发生免疫交叉反应。在兔网织红细胞无细胞系统中，TA5未抑制A链的酶活性。已证明TB12与B链的半乳糖结合位点发生反应。TA5和TB12与植物毒素蓖麻毒素未显示交叉反应。已测定单克隆抗体的缔合常数。讨论了欧洲槲寄生凝集素异质性的性质。