The Journal of Biochemistry
Online ISSN : 1756-2651
Print ISSN : 0021-924X
Purification and Characterization of β-Mannosidase from Human Placenta
Yuji IwasakiAkihiko TsujiKiyoshi OmuraYoshiyuki Suzuki
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1989 Volume 106 Issue 2 Pages 331-335


Lysosomal β-mannosidase was purified almost 10, 000-fold from human placenta. The final preparation showed several protein bands on polyacrylamide gel electrophoresis. Its molecular mass was estimated to be 110 kDa, the optimal pH was 4.5, the Km was 0.56 mM, and the isoelectric point was 4.7. The enzyme was found to bind completely to Con A-Sepharose, and the pI was not changed after neuraminidase treatment. These results indicate that the purified enzyme represents a lysosomal form which contains high mannose type oligosaccharide chains and only a few sialic acids, if any.

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