Efficient purification of a full length and biochemically active p110Rb, the retinoblastoma gene product
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Real-time Analyses of Retinol Transport by the Membrane Receptor of Plasma Retinol Binding Protein
Published on: January 28, 2013
E Savoysky1, M Suzuki, K Tamai
1Laboratory of Cancer Cell Biology, Nagoya University School of Medicine, Japan.
Abstract:
Rb protein was purified from recombinant baculovirus-infected Sf9 cells to apparent homogeneity by a simple solubilization and by immunoaffinity column chromatography. It was mainly obtained as p110Rb, the underphosphorylated form of the Rb protein family. This p110Rb was shown to form a specific complex in vitro with SV40 Tag and to bind to double or single stranded DNA. It could also affect Tag helicase activity in a biphasic-dose dependent manner, due to these two biochemical functions. This purification procedure provides sufficient amounts of native Rb protein to further elucidate its role as an anti-oncogene protein and a negative regulator of the cell cycle.
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The first-ever tumor suppressor gene called Rb was identified in retinoblastoma - a rare eye tumor in children. In inherited forms of the disease, a child inherits one defective copy of the Rb gene, which predisposes them to retinoblastoma. However,...