Biopolym. Cell. 2004; 20(6):493-497.
Structure and Function of Biopolymers
Purification and properties of the lectins from aerial part of three species of plants genus hawkweed (Hieracium)
1Antonyuk V. A.
  1. Institute of Cell Biology, NAS of Ukraine
    14/16, Drahomanov Str., Lviv, Ukraine, 79005

Abstract

From aerial part of three species of the plants of genus hawkweed (Hieracium aurantiacum, H. pilosella, H. sylvularum), family Asteraceae, the lectins have been purified with the yield of 61, 126 and 92 mg per kg of crude drugs, accordingly. The molecular mass of the three lectins as determined by gel filtration on Toyopearl HW-55 is 36 kDa. According to the SDS-PAGE data, the lectins contain one component of molecular mass approximately 18 kDa. The PAGE disc electrophoresis in an alkaline (pH 8.9) and acidic systems (pH 4.3) detected one protein band, that presumes the lectins investigated to consist of one isoform. The sugar component (2.1–2.2 %) was revealed in the lectins. The lectins of three species studied agglutinate rabbit erythrocytes best of all and agglutinate weaker hen, sheep and human erythrocytes. The best inhibitor of lectin activity for three species of genus hawkweed is N,N'‚N'''‚N'''-tetraacethylchitotetraose. This sugar is 8 time stronger inhibitor than N,N'-diacethylchitobiose and 625 time stronger than N-acethyl-D-glucosamine. Peroxidase-lectin conjugates and FITC-labelled lectins for histochemicals applications have been prepared.

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