TY - JOUR
T1 - Efficient purification of a full length and biochemically active p110Rb, the retinoblastoma gene product
AU - Savoysky, Ericka
AU - Suzuki, Motoshi
AU - Tamai, Katsuyuki
AU - Sakurai, Takeshi
AU - Ohuchi, Tohru
AU - Akiyama, Tetsu
AU - Kojima, Kyohide
AU - Yoshida, Shonen
N1 - Funding Information:
We thank Drs K.T. Koizumi, S. Izuta and Mrs C. Simbulan in our laboratory, and Dr. Kumao Toyoshima of Department of Gncogene Research, Institute for Microbial Diseases, for their helpful discussions. This work was supported by post-doctoral fellowships from the Japanese Society for Promotion of Science and from the French Ministry for Foreign Affairs (Bourses Lavoisier), and also partly supported by a Grant-in-Aid for Cancer Research from the Ministry of Education, Science and Culture of Japan.
PY - 1992/9/16
Y1 - 1992/9/16
N2 - 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.
AB - 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.
UR - https://www.scopus.com/pages/publications/0026804667
UR - https://www.scopus.com/pages/publications/0026804667#tab=citedBy
U2 - 10.1016/0006-291X(92)91251-K
DO - 10.1016/0006-291X(92)91251-K
M3 - Article
C2 - 1530627
AN - SCOPUS:0026804667
SN - 0006-291X
VL - 187
SP - 697
EP - 702
JO - Biochemical and Biophysical Research Communications
JF - Biochemical and Biophysical Research Communications
IS - 2
ER -