scholarly journals Purification and properties of a high molecular weight acid soluble nuclear protein from mouse ascites sarcoma cells

1978 ◽  
Vol 90 (7-8) ◽  
pp. 999-1013
Author(s):  
Kimiko TSUTSUI
1975 ◽  
Vol 151 (2) ◽  
pp. 227-238 ◽  
Author(s):  
A G McLennan ◽  
H M Keir

Two DNA polymerases of high molecular weight, pol A (mol.wt. 190 000) and pol B (mol.wt. 240 ooo), have been purified 6300-fold and 1600-fold respectively from an extramitochondrial supernatant of a bleached strain of Euglena gracilis. They have very similar requirements when assayed with an ‘activated’-DNA primer-template [the optimum conditions of pH and ionic (K+ and Mn2+) composition being 7.2, 25 mM and 0.2 mM respectively]. 0.2 mM-Mn2+ was about 1.5-2-fold as effective as 2 mM-Mg2+, owing to substrate activation by deoxyribonucleoside 5′-triphosphates in the presence of Mn2+. Km values for the triphosphates in the absence of activation were about 10(-6)M with Mn2+ and 8 × 10(-6) M with Mg2+ for both enzymes. They were inhibited to the same extent by N-ethylmaleimide, novobiocin and o-phenanthroline, but differed in their chromatographic behaviour on DEAE-cellulose and in their electrophoretic mobilities on polyacrylamide gel. No evidence was found for the existence in these cells of a DNA polymerase of low molecular weight, but there were indications that a third enzyme of high molecular weight might exist.


1974 ◽  
Vol 38 (5) ◽  
pp. 947-952 ◽  
Author(s):  
Mamoru SUGIURA ◽  
Masakazu ISOBE ◽  
Noriyuki MUROYA ◽  
Tsutomu YAMAGUCHI

1996 ◽  
Vol 7 (8) ◽  
pp. 1249-1258 ◽  
Author(s):  
G Pintucci ◽  
N Quarto ◽  
D B Rifkin

The high molecular weight (HMW) forms (24, 22.5, and 22 kDa) of basic fibroblast growth factor-2 (FGF-2) contain an N-terminal extension responsible for their predominantly nuclear localization. These forms of FGF-2 are post-translationally modified, resulting in a 1- to 2-kDa increase in apparent molecular mass. Here we show that this post-translational modification is inhibited by methionine starvation and by the methyltransferase inhibitors 5'-deoxy-5'-methylthioadenosine (MTA) and 3-deaza-adenosine. Inhibition of the methylation-dependent modification results in a significant decrease in HMW FGF-2 nuclear accumulation, suggesting that methylation is relevant to the intracellular distribution of these forms of FGF-2. Treatment with MTA does not affect either the synthesis or the intracellular fate of another nuclear protein, the SV40 large T antigen, demonstrating that this drug does not have a generalized effect on nuclear protein accumulation. These results link HMW FGF-2 post-translational modification to its intracellular distribution.


2001 ◽  
Vol 29 (1) ◽  
pp. 70-75 ◽  
Author(s):  
Tohru Kobayashi ◽  
Norihiko Higaki ◽  
Atsushi Suzumatsu ◽  
Kazuhisa Sawada ◽  
Hiroshi Hagihara ◽  
...  

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