Abstract
Isolation of soybean agglutinin (SBA) by the salt fractionation involves excessive amounts of (NH4)2SO4. 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 degrees C and 25 degrees 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)2SO4 method as ascertained by chromatographic and electrophoretic comparisons and hapten inhibition assays.
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