Efficient purification of a full length and biochemically active p110Rb, the retinoblastoma gene product

Ericka Savoysky, Motoshi Suzuki, Katsuyuki Tamai, Takeshi Sakurai, Tohru Ohuchi, Tetsu Akiyama, Kyohide Kojima, Shonen Yoshida

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10 Citations (Scopus)


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.

Original languageEnglish
Pages (from-to)697-702
Number of pages6
JournalBiochemical and Biophysical Research Communications
Issue number2
Publication statusPublished - 16-09-1992


All Science Journal Classification (ASJC) codes

  • Biophysics
  • Biochemistry
  • Molecular Biology
  • Cell Biology

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