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Abstract
Isolation of soybean agglutinin (SBA) by the salt fractionation involves excessive amounts of (NH4) 2 SO 4. We have found that SBA could be fractionally precipitated from an aqueous extract by adding acetone (40% final concentration). It is stable under these conditions for minimum 2 h at 5°C and 25°C. Incorporating these results, an improved procedure for the isolation of SBA has been developed. The SBA isolated by this method is obtained in better yield, has 6000 HU/mg protein and is identical to that isolated by the (NH4)2 SO 4 method as ascertained by chromatographic and electro-phoretic comparisons and hapten inhibition assays.