Lysosomal neuraminidase and beta-galactosidase are present in a complex together with a 32-kDa protective protein. This complex has been purified and the different components have been dissociated using potassium isothiocyanate (KSCN) treatment. beta-Galactosidase remains catalytically active, but neuraminidase loses its activity upon dissociation. The inactive dissociated neuraminidase was purified by removing the remaining non-dissociated beta-galactosidase/protective protein complex using beta-galactosidase-specific affinity chromatography. The dissociated neuraminidase material shows two major polypeptides on SDS-PAGE with an apparent molecular mass of 76 kDa and 66 kDa. Subsequently the 32-kDa protective protein was dissociated from the beta-galactosidase/protective protein complex, and purified. Antibodies raised against the dissociated inactive neuraminidase preparation specifically immunoprecipitate the active neuraminidase present in the complex with beta-galactosidase and protective protein. By immunoblotting evidence is provided that the 76-kDa protein is a subunit of neuraminidase which, in association with the 32-kDa protective protein, is essential for neuraminidase activity.
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|Titolo:||Purification and partial characterization of lysosomal neuraminidase from human placenta.|
|Rivista:||EUROPEAN JOURNAL OF BIOCHEMISTRY|
|Citazione:||Verheijen, F.w., Palmeri, S., Hoogeveen, A.t., & Galjaard, H. (1985). Purification and partial characterization of lysosomal neuraminidase from human placenta. EUROPEAN JOURNAL OF BIOCHEMISTRY, 149(2), 315-321.|
|Appare nelle tipologie:||1.1 Articolo in rivista|