scholarly journals Association of initiation factor eIF-2 with a rapidly sedimenting fraction from Ehrlich ascites-tumour cells

1981 ◽  
Vol 194 (1) ◽  
pp. 357-360 ◽  
Author(s):  
M J Clemens ◽  
V M Pain
Keyword(s):  
Protein Synthesis ◽  
Subcellular Distribution ◽  
Microsomal Fraction ◽  
Initiation Factor ◽  
Ascites Cell ◽  
Ehrlich Ascites ◽  
Ehrlich Ascites Tumour ◽  
Ehrlich Ascites Cell ◽  
Ascites Tumour Cells ◽  
Ehrlich Ascites Tumour Cells

To determine the subcellular distribution of initiation-factor eIF-2 activity, Ehrlich ascites-cell homogenates were fractionated to give (a) a rapidly sedimenting fraction, (b) a microsomal fraction and (c) post-microsomal supernatant. The first two fractions were washed in 0.5 m-KCl to render the associated protein-synthesis factor soluble. As much as 60% of the total recoverable eIF-2 was obtained from the rapidly sedimenting material.

scholarly journals Substrate-dependent utilization of the glycerol 3-phosphate or malate/aspartate redox shuttles by Ehrlich ascites cells

1995 ◽  
Vol 310 (2) ◽  
pp. 665-671 ◽  
Author(s):  
A R Grivell ◽  
E I Korpelainen ◽  
C J Williams ◽  
M N Berry
Keyword(s):  
Isolated Hepatocytes ◽  
Dihydroxyacetone Phosphate ◽  
Ehrlich Ascites ◽  
Reducing Equivalent ◽  
Redox Shuttles ◽  
Ehrlich Ascites Tumour ◽  
Ehrlich Ascites Cell ◽  
Ascites Tumour Cells ◽  
Ehrlich Ascites Tumour Cells ◽  
Reducing Equivalents

The rate of transfer of reducing equivalents from cytoplasm to mitochondria has been examined in Ehrlich ascites tumour cells incubated in the presence of lactate. The flux of reducing equivalents was determined from the rate of metabolism of reduced intermediates that are oxidized within the cytosol. The magnitude of the flux of reducing equivalents was dependent on both the concentration of added lactate and the presence of carbohydrate. The rate of flux was twice as great in the presence of glucose and four times as high when glucose and lactate were added together as when lactate was the only added substrate. Fructose was less effective than glucose in stimulating reducing equivalent flux. In the presence of glucose or fructose, there was a substantial accumulation of hexose phosphates, dihydroxyacetone phosphate and glycerol 3-phosphate. Rotenone, an inhibitor of NADH dehydrogenase, and amino-oxyacetate, which inhibits the malate/aspartate shuttle, were powerful suppressors of reducing equivalent flux from lactate as sole substrate, but were much less potent in the presence of carbohydrate. Antimycin substantially inhibited reducing equivalent flux from all combinations of added substrates, consistent with its ability to block oxidation of reducing equivalents transferred by both the malate/aspartate and glycerol 3-phosphate shuttles. The glycerol 3-phosphate shuttle represents around 80% of the maximum total observed activity but is active only while glycolytic intermediates are present to provide the necessary substrates of the shuttle. This Ehrlich ascites cell line has an essentially similar total reducing equivalent shuttle capacity to that of isolated hepatocytes.

Regulation of protein synthesis in Ehrlich ascites tumour cells in culture

1980 ◽  
Vol 8 (3) ◽  
pp. 286-287 ◽  
Author(s):  
EDGAR C. HENSHAW ◽  
MICHAEL CENTRELLA ◽  
WALTER MASTROPAOLO ◽  
KELVIN E. SMITH ◽  
SIE TING WONG
Keyword(s):  
Protein Synthesis ◽  
Tumour Cells ◽  
Ascites Tumour ◽  
Cells In Culture ◽  
Ehrlich Ascites ◽  
Ehrlich Ascites Tumour ◽  
Ascites Tumour Cells ◽  
Ehrlich Ascites Tumour Cells
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