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 Purification and properties of a novel Ca2+-binding protein (10.5 kDa) from Ehrlich-ascites-tumour cells

1987 ◽  
Vol 247 (3) ◽  
pp. 663-667 ◽  
Author(s):  
J Kuźnicki ◽  
A Filipek
Keyword(s):  
Binding Protein ◽  
Polyacrylamide Gel Electrophoresis ◽  
Tumour Cells ◽  
Ascites Tumour ◽  
Tyrosine Fluorescence ◽  
Purification And Properties ◽  
Ehrlich Ascites ◽  
Ehrlich Ascites Tumour ◽  
Ascites Tumour Cells ◽  
Ehrlich Ascites Tumour Cells

A novel Ca2+-binding protein (CaBP) was identified in Ehrlich-ascites-tumour cells and purified to homogeneity. The molecular mass of this protein is about 10.5 kDa as estimated by polyacrylamide-gel electrophoresis in the presence of SDS. CaBP has two Ca2+-binding sites that bind Ca2+ with a dissociation constant of about 3 × 10(-6)M. Ca2+ binding to CaBP decreases its electrophoretic mobility in urea/polyacrylamide gels, changes its u.v. spectrum, increases the intrinsic tyrosine fluorescence intensity and strengthens hydrophobic interaction with the phenyl-Sepharose matrix.

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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