Mature beta-hexosaminidase A has been found associated to the external leaflet of plasma membrane of cultured fibroblasts. The plasma membrane association of P-hexosaminidase A has been directly determined by cell surface biotinylation followed by affinity chromatography purification of the biotinylated proteins, and by immunocytochemistry. The immunological and biochemical characterization of biotinylated beta-hexosaminidase A revealed that the plasma membrane associated enzyme is fully processed, suggesting its lysosomal origin. (c) 2005 Published by Elsevier B.V. on behalf of the Federation of European Biochemical Societies.
Identification of plasma membrane associated mature β-hexosaminidase A, active towards GM2 ganglioside, in human fibroblasts / S. Mencarelli, C. Cavalieri, A. Magini, B. Tancini, L. Basso, P. Lemansky, A. Hasilik, Y.T. Li, V. Chigorno, A. Orlacchio, C. Emiliani, S. Sonnino. - In: FEBS LETTERS. - ISSN 0014-5793. - 579:25(2005 Oct 24), pp. 5501-5506. [10.1016/j.febslet.2005.08.081]
Identification of plasma membrane associated mature β-hexosaminidase A, active towards GM2 ganglioside, in human fibroblasts
V. Chigorno;S. SonninoUltimo
2005
Abstract
Mature beta-hexosaminidase A has been found associated to the external leaflet of plasma membrane of cultured fibroblasts. The plasma membrane association of P-hexosaminidase A has been directly determined by cell surface biotinylation followed by affinity chromatography purification of the biotinylated proteins, and by immunocytochemistry. The immunological and biochemical characterization of biotinylated beta-hexosaminidase A revealed that the plasma membrane associated enzyme is fully processed, suggesting its lysosomal origin. (c) 2005 Published by Elsevier B.V. on behalf of the Federation of European Biochemical Societies.
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