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beta-D-Mannosidase was partially purified (108-fold) from human placenta by ammonium sulfate precipitation, Concanavalin A-Sepharose affinity chromatography, gel filtration and hydroxylapatite chromatography. Further attempts to purify the enzyme by several conventional methods failed due to loss of activity. The stability of beta-mannosidase, the effect of several compounds on its activity and some physico-chemical and kinetic parameters were investigated.

β-D-Mannosidase from Human Placenta: Properties and Partial Purification