beta-D-Mannosidase from human placenta: properties and partial purification.

C Noeske; G Mersmann

doi:10.1515/bchm2.1983.364.2.1645

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beta-D-Mannosidase from human placenta: properties and partial purification.

C Noeske·G Mersmann

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Abstract

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.

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Chromatography, Affinity Chromatography, Gel Female Humans Kinetics Mannosidases Molecular Weight Placenta Pregnancy beta-Mannosidase Journal Article

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C Noeske, G Mersmann. 1983. beta-D-Mannosidase from human placenta: properties and partial purification.. https://doi.org/10.1515/bchm2.1983.364.2.1645

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