We previously reported the isolation of a sialic acid-specific lectin eluted from the bark of Maackia fauriei using alkaline buffer on a fetuin-affinity column. Application of a borate-based elution buffer in the present study increased the specific activity of purified lectin from crude protein extract by 2.6-fold, whilst only slightly decreasing the recovery by 1.13%. The biological properties of the lectin eluted with borate buffer were the same as those of the lectin eluted with alkaline buffer such as in terms of the hemagglutination activity, hemagglutination inhibition activity, molecular mass, purity, and cytotoxicity to human breast cancer cells. A prepared biotin-labeled lectin conjugate was used to investigate the binding to various glycoproteins. Our results indicate that eluting with borate buffer is more efficient than using alkaline buffer to isolate the lectin adsorbed in a fetuin-affinity column.