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Table 1 Specific hemagglutinating activities and yields of chromatographic fractions obtained at different steps of purification of lectin

From: Purification and characterization of a novel plant lectin from Pinellia ternata with antineoplastic activity

Fraction

Total protein(mg)

Specific hemagglutinating activity (HA/mg)

Total activity by HA

Purification fold

Recovery of protein (%)

Crude extract

2600

8.75

22750

1

100

hydrophobic chromatography

235

65.83

15470

7.5

9.04

ion-exchange chromatography

74

125.41

9280

14.3

2.85

  1. Purification was initiated from 100 g of bulbs of Pinellia ternata, a lectin from Pinellia ternata was purified by a combination of ion exchange and hydrophobic chromatographic steps, which revealed strong agglutination activity with Kunming mouse erythrocytes. Hemagglutinating activity test was employed to monitor all the purification procedure. The total activity was measured by hemagglutinating activity assay as described in “materials and methods” section.
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