1996 Volume 60 Issue 4 Pages 666-668
We purified an enzyme hydrolyzing 2-sulfo-α-L-fucopyranose pyridylaminiated 2-sulfo-α-L-fucopyranosyl-(1→2)-fucose from the acetone powder of the digestive tract of a sea urchin. The enzyme was purified 307-fold with an overall recovery of 1.63% by ammonium sulfate precipitation, cation exchange chromatography, and gel filtration chromatography. The enzyme is useful for the structural analysis of sulfated fucan.
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