Calcium-binding protein from mouse Ehrlich ascites-tumour cells is homologous to human calcyclin.
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.
Kuźnicki
J
J
Nencki Institute of Experimental Biology, Department of Muscle Biochemistry, Warszawa, Poland.
Filipek
A
A
Hunziker
P E
PE
Huber
S
S
Heizmann
C W
CW
D000595:Amino Acid Sequence; D000596:Amino Acids / Q000032:analysis; D000818:Animals; D001345:Autoradiography; D015153:Blotting, Western; D002135:Calcium-Binding Proteins / Q000032:analysis*; D002286:Carcinoma, Ehrlich Tumor / Q000032:analysis*; D018797:Cell Cycle Proteins; D002851:Chromatography, High Pressure Liquid; D051379:Mice; D008969:Molecular Sequence Data; D010449:Peptide Mapping; D000075383:S100 Calcium Binding Protein A6; D009418:S100 Proteins; D014357:Trypsin
D000596:Amino Acids; D002135:Calcium-Binding Proteins; D018797:Cell Cycle Proteins; D000075383:S100 Calcium Binding Protein A6; D009418:S100 Proteins; C489134:S100a6 protein, mouse; C489132:S100a6 protein, rat; D014357:Trypsin