scholarly journals Calcium Binding in Homogenates of Ehrlich Ascites Tumour Cells

Nature ◽  
1960 ◽  
Vol 186 (4725) ◽  
pp. 656-656
Author(s):  
R. SCHOFIELD ◽  
D. THOMASON
Keyword(s):  
Calcium Binding ◽  
Tumour Cells ◽  
Ascites Tumour ◽  
Ehrlich Ascites ◽  
Ehrlich Ascites Tumour ◽  
Ascites Tumour Cells ◽  
Ehrlich Ascites Tumour Cells

scholarly journals Calcium-binding protein from mouse Ehrlich ascites-tumour cells is homologous to human calcyclin

1989 ◽  
Vol 263 (3) ◽  
pp. 951-956 ◽  
Author(s):  
J Kuźnicki ◽  
A Filipek ◽  
P E Hunziker ◽  
S Huber ◽  
C W Heizmann
Keyword(s):  
Calcium Binding ◽  
Binding Protein ◽  
Tumour Cells ◽  
Ascites Tumour ◽  
Ehrlich Ascites ◽  
Ehrlich Ascites Tumour ◽  
S 100 ◽  
Cycle Regulation ◽  
Ascites Tumour Cells ◽  
Ehrlich Ascites Tumour Cells

A Ca2+-binding protein was purified from mouse Ehrlich ascites-tumour cells. The protein forms monomers and disulphide-linked dimers, which can be separated by reverse-phase h.p.l.c. A partial amino acid sequence analysis demonstrated that the protein has an EF-hand structure. A striking homology was found to rat and human calcyclin (a member of the S-100 protein family), which is possibly involved in cell-cycle regulation.

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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