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Updated: Aug 15, 2026

Isolation of Labile Multi-protein Complexes by in vivo Controlled Cellular Cross-Linking and Immuno-magnetic Affinity Chromatography
Published on: March 10, 2010
Mannosylphosphodolichol synthase activity is associated with a 32 kDa phosphoprotein
D K Banerjee1, J J DaSilva, B Bigio
1Department of Biochemistry, School of Medicine, University of Puerto Rico, San Juan 00936-5067, USA. d.banerjee@remaca.upr.ciu.edu
Abstract:
Failure of actinomycin D to block the activation of Dol-P-Man synthase in isoproterenol-treated capillary endothelial cells, supported that isoproterenol effect was not mediated by active transcription of the Dol-P-Man synthase gene during a short-term beta-adrenoreceptor stimulation. Instead, it was a net effect of protein phosphorylation by cAMP-dependent protein kinase. Using antibody as a probe we have now demonstrated that Dol-P-Man synthase activity is associated with a 32 kDa ER phosphoprotein.
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