Abstract
Publisher Summary The blood or hemolymph of the Californian coastal crab Cancer antennarius Stimpson contains a sialic acid-specific lectin with high affinity for 9- O -acetyl- and 4-O-acetyl- N -acetylneuraminic acids. This chapter describes a method of purification using bovine submaxillary mucin-Sepharose as an affinity absorbent. There is also a description of the properties of the lectin. The activity of the crab lectin is assayed by measuring its ability to agglutinate horse (rat or mouse) erythrocytes. The assay is done by the conventional procedure of serial 2-fold dilution of the lectin on microtiter plates and visual estimation of erythrocyte agglutination l hr after adding the cells. The crab lectin is purified using an affinity adsorbent of bovine submaxillary mucin (BSM) coupled to Sepharose because the lactin exhibits high binding affinity for the O-acetylated sialic acids in BSM.
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