Calcyclin from mouse Ehrlich ascites tumor cells and rabbit lung form non-covalent dimers.
Crosslinking treatments of fresh cytosol from mouse Ehrlich ascites tumor (EAT) cells revealed the existence of calcyclin dimers which were sensitive to SDS, but not to reducing agents, which suggests the existence of non-covalent dimers. In stored EAT cell cytosol and preparations of purified calcyclin dimers were also formed by S-S bridging (covalent dimers). The S-S dimers did not bind to organomercurial Agarose and could be separated from reduced forms of calcyclin that bound to the resin. Calcyclin eluted from the resin with DTT was a mixture of monomers and non-covalent dimers as shown by crosslinking and subsequent immunoblotting. Calcyclin from rabbit lung, lacking a cysteine residue, could also be crosslinked as a dimer. It is suggested that the ability of calcyclin to form non-covalent dimers is of physiological significance.
Wojda
U
U
Nencki Institute of Experimental Biology, Warsaw, Poland.
Kuźnicki
J
J
D000818:Animals; D002135:Calcium-Binding Proteins / Q000737:chemistry* / Q000302:isolation & purification; D002286:Carcinoma, Ehrlich Tumor / Q000737:chemistry; D018797:Cell Cycle Proteins; D008168:Lung / Q000737:chemistry; D051379:Mice; D011817:Rabbits; D000075383:S100 Calcium Binding Protein A6; D009418:S100 Proteins; D014407:Tumor Cells, Cultured
D002135:Calcium-Binding Proteins; D018797:Cell Cycle Proteins; D000075383:S100 Calcium Binding Protein A6; D009418:S100 Proteins; C489134:S100a6 protein, mouse