Purified DNA polymerases α, σ, and ε from the highly malignant Novikoff hepatoma cells have lowered copying fidelity

1995 ◽  
Vol 121 (S1) ◽  
pp. A16-A16
Author(s):  
G. Fox ◽  
O. Popanda ◽  
H. W. Thielmann
Keyword(s):  
Dna Polymerases ◽  
Hepatoma Cells ◽  
Novikoff Hepatoma ◽  
Copying Fidelity

Evidence for reduced copying fidelity of DNA polymerases α, δ, and ε from Novikoff hepatoma cells

1997 ◽  
Vol 123 (11-12) ◽  
pp. 659-668 ◽  
Author(s):  
Gabriele Fox ◽  
Odilia Popanda ◽  
H. W. Thielmann
Keyword(s):  
Dna Polymerases ◽  
Hepatoma Cells ◽  
Novikoff Hepatoma ◽  
Copying Fidelity

Preferential inhibition of DNA polymerases?,?, and? from Novikoff hepatoma cells by inhibitors of cell proliferation

1996 ◽  
Vol 122 (2) ◽  
pp. 78-94 ◽  
Author(s):  
Gabriele Fox ◽  
Odilia Popanda ◽  
Lutz Edler ◽  
Heinz Walter Thielmann
Keyword(s):  
Cell Proliferation ◽  
Dna Polymerases ◽  
Hepatoma Cells ◽  
Novikoff Hepatoma

Initiation of transcription in permeabilized novikoff hepatoma cells

1980 ◽  
Vol 4 (2) ◽  
pp. 175-184 ◽  
Author(s):  
B SAMAL ◽  
N BALLAL ◽  
H BUSCH
Keyword(s):  
Hepatoma Cells ◽  
Novikoff Hepatoma ◽  
Initiation Of Transcription

scholarly journals Photoaffinity labelling of a nitrobenzylthioinosine-binding polypeptide from cultured Novikoff hepatoma cells

1986 ◽  
Vol 236 (3) ◽  
pp. 665-670 ◽  
Author(s):  
W P Gati ◽  
J A Belt ◽  
E S Jakobs ◽  
J D Young ◽  
S M Jarvis ◽  
...  
Keyword(s):  
Gel Electrophoresis ◽  
Plasma Membranes ◽  
Specific Binding ◽  
Polyacrylamide Gel Electrophoresis ◽  
Sodium Dodecyl ◽  
Hepatoma Cells ◽  
Nucleoside Transport ◽  
Facilitated Diffusion ◽  
Animal Cells ◽  
Novikoff Hepatoma

Site-specific binding of nitrobenzylthioinosine (NBMPR) to plasma membranes of some animal cells results in the inhibition of the facilitated diffusion of nucleosides. The present study showed that nucleoside transport in Novikoff UA rat hepatoma cells is insensitive to site-saturating concentrations of NBMPR. Equilibrium binding experiments demonstrated the presence of high-affinity sites for NBMPR in a membrane-enriched fraction from these cells. In the presence of uridine or dipyridamole, specific binding of NBMPR at these sites was inhibited. When Novikoff UA membranes were covalently labelled with [3H]NBMPR by using photoaffinity techniques, specifically bound radioactivity was incorporated exclusively into a polypeptide(s) with an apparent Mr of 72,000-80,000, determined by sodium dodecyl sulphate/polyacrylamide-gel electrophoresis. Covalent labelling of this polypeptide was abolished in the presence of excess nitrobenzylthioguanosine (NBTGR) and reduced in the presence of adenosine, uridine or dipyridamole. The apparent Mr of the NBMPR-binding polypeptide in Novikoff UA cells is significantly higher than that reported for corresponding polypeptides in other cell types (Mr 45,000-66,000). When membrane-enriched preparations from S49 mouse lymphoma cells were photolabelled and mixed with labelled NovikoffUA membrane-enriched preparations, gel electrophoresis resolved the NBMPR-binding polypeptides from the two preparations.

Diversity in rat strains and tumor lines of DNA fragments homologous to an amplified 5.8 kilobase Eco R1 fragment of Novikoff hepatoma cells

1981 ◽  
Vol 101 (2) ◽  
pp. 639-644
Author(s):  
Lawrence I. Rothblum ◽  
David L. Parker ◽  
Brandt Cassidy ◽  
Frederick F. Becker ◽  
Harris Busch ◽  
...  
Keyword(s):  
Hepatoma Cells ◽  
Dna Fragments ◽  
Rat Strains ◽  
Novikoff Hepatoma
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