scholarly journals Poly(ADP-ribose) polymerase from Ehrlich ascites-tumour cells. Amino acid composition, N-terminal analysis and chemical cleavage of the purified protein

1980 ◽  
Vol 185 (3) ◽  
pp. 779-782 ◽  
Author(s):  
J Holtlund ◽  
T Kristensen ◽  
K Sletten
Keyword(s):  
Amino Acids ◽  
Amino Acid ◽  
Amino Acid Composition ◽  
Acid Composition ◽  
Ascites Tumour ◽  
Ehrlich Ascites ◽  
Ehrlich Ascites Tumour ◽  
Terminal Amino ◽  
Ascites Tumour Cells ◽  
Ehrlich Ascites Tumour Cells

Poly(ADP-ribose) polymerase was purified from Ehrlich ascites-tumour cells by two novel methods. Analysis for amino acid composition revealed a high percentage of acidic amino acids or their amides, and of basic amino acids. N-Terminal analysis with dansyl chloride revealed no terminal amino acid, indicating a blocked N-terminal amino group. Analysis by gel electrophoresis of protein treated with 3-bromo-3-methyl-2-[(2-nitrophenylthio)-3H-indole, under conditions where selective cleavage of the polypeptide chain at tryptophan residues is obtained, showed six major peptide bands.

scholarly journals The transport and oxidation of succinate by Ehrlich ascites-tumour cells

1976 ◽  
Vol 160 (1) ◽  
pp. 121-123 ◽  
Author(s):  
T L Spencer
Keyword(s):  
Ph Dependence ◽  
Organic Anion ◽  
Tumour Cells ◽  
Cell Integrity ◽  
Carrier System ◽  
Ascites Tumour ◽  
Ehrlich Ascites ◽  
Ehrlich Ascites Tumour ◽  
Ascites Tumour Cells ◽  
Ehrlich Ascites Tumour Cells

The transport and oxidation of succinate by functionally intact Ehrlich ascites-tumour cells was investigated. On the basis of pH dependence and inhibitor sensitivity it was concluded that succinate may be transported across the cell membrane by the organic anion carrier system. Thus the ability of isolated Ehrlich cells to oxidize succinate is real, and is not necessarily a result of damage to cell integrity.

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