[使用单克隆抗体对槲寄生植物凝集素的研究]

[Study of plant lectins from Viscum album using monoclonal antibodies].

作者信息

Tonevitskiĭ A G, Rakhmanova V A, Shamshiev A T, Usachaeva E A, Agapov I I, Prokov'ev S A, Denisenko O N, Pfuller U, Eifler R

机构信息

Witten-Herdex University, Germany.

出版信息

Mol Biol (Mosk). 1995 May-Jun;29(3):619-26.

PMID:8552066

Abstract

Monoclonal antibodies (monAT) against both native (TA5, TB12) and denatured (TB33, TB35) plant toxin ML1 from Viscum album have been obtained. The interaction of monAT against native toxin with its isoforms ML2 and ML3 was investigated. It was shown that monAT TA5 to A-chain of ML1 toxin cross-reacted with ML2 and ML3 isoforms. TA5 did not inhibit enzyme activity of A-chain in cell-free rabbit reticulocyte system. It was shown that monAT TB12 reacted with galactose-binding site of B-subunit. Both monAT had no cross-reactions with plant toxin ricin. The binding constants for TA5 with ML1, ML2, ML3 respectively were 4.3.10(7) M-1, 1.2.10(7) M-1, and 0.3.10(7) M-1. The binding constants for TB12 were 2.10(7) M-1 with ML1 toxin, and more than 10(6) M-1 with ML2 and ML3. The nature of heterogeneity in ML toxin family is discussed. Test-systems for ML1 determination in different V. album extracts are suggested.

摘要

已获得针对来自欧洲槲寄生的天然（TA5、TB12）和变性（TB33、TB35）植物毒素ML1的单克隆抗体（monAT）。研究了针对天然毒素的单克隆抗体与其同工型ML2和ML3的相互作用。结果表明，针对ML1毒素A链的单克隆抗体TA5与ML2和ML3同工型发生交叉反应。TA5在无细胞兔网织红细胞系统中不抑制A链的酶活性。结果表明，单克隆抗体TB12与B亚基的半乳糖结合位点发生反应。两种单克隆抗体均与植物毒素蓖麻毒素无交叉反应。TA5与ML1、ML2、ML3的结合常数分别为4.3×10⁷ M⁻¹、1.2×10⁷ M⁻¹和0.3×10⁷ M⁻¹。TB12与ML1毒素的结合常数为2×10⁷ M⁻¹，与ML2和ML3的结合常数大于10⁶ M⁻¹。讨论了ML毒素家族异质性的本质。提出了用于测定不同欧洲槲寄生提取物中ML1的检测系统。