Investigation of plant lectins from Viscum album by monoclonalantibodies.

Journal/Book: MOL-BIOL, 1995, Vol/Iss/Pg. 29/3 (619-626), ISSN: 0026-8984, Full Title:Molekulyarnaya Biologiya.. 1995;

Abstract: Monoclonal antibodies (monAT) against both native (TA5, TB12) anddenatured (TB33, TB35) plant toxin ML1 from Viscum album have beenobtained. The interaction of monAT against native toxin with itsisoforms ML2 and ML3 was investigated. It was shown that monAT TA5 toA-chain of ML1 toxin cross-reacted with ML2 and ML3 isoforms. TA5 didnot inhibit enzyme activity of A-chain in cell-free rabbit reticulocytesystem. It was shown that monAT TB12 reacted with galactose-binding siteof B-subunit. Both monAT had no cross-reactions with plant toxin ricin.The binding constants for TA5 with ML1, ML2, ML3 respectively were4.3midline dot107 M-1, 1.2midline dot107 M-1, and 0.3midline dot107 M-1.The binding constants for TB12 were 2midline dot107 M-1 with ML1 toxin,and more than 106 M-1 with ML2 and ML3. The nature of heterogeneity inML toxin family is discussed. Test-systems for ML1 determination indifferent V. album extracts are suggested.

Keyword(s): Medical:enzyme-activity

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