Ca2+-dependent interaction of calcyclin with membrane.
The presence of calcyclin in the microsomal fraction of Ehrlich ascites tumor cells was detected using polyclonal antibodies. Association of calcyclin with the microsomes depended on the presence of calcium ions in the buffer used for cell fractionation. The interaction of calcylcin with Ehrlich ascites tumor cells microsomes was confirmed in the in vitro conditions by cosedimentation assay using exogenous calcyclin. It was shown that phospholipids extracted from natural membranes and purified phosphatydylserine or phosphatydylcholine were not involved in the binding. Instead, several low molecular weight polypeptides in the Triton X-100 resistant membrane fraction were found to interact with calcyclin.
Lesniak
W
W
Department of Muscle Biochemistry, Nencki Institute of Experimental Biology, Warsaw, Poland.
Filipek
A
A
D000818:Animals; D002118:Calcium / Q000494:pharmacology*; D002135:Calcium-Binding Proteins / Q000032:analysis / Q000378:metabolism*; D002286:Carcinoma, Ehrlich Tumor / Q000648:ultrastructure; D018797:Cell Cycle Proteins; D002462:Cell Membrane / Q000378:metabolism*; D004533:Egtazic Acid / Q000494:pharmacology; D008081:Liposomes / Q000378:metabolism; D008565:Membrane Proteins / Q000378:metabolism; D051379:Mice; D008861:Microsomes / Q000378:metabolism / Q000648:ultrastructure; D008970:Molecular Weight; D017830:Octoxynol / Q000494:pharmacology; D010743:Phospholipids / Q000378:metabolism; D000075383:S100 Calcium Binding Protein A6; D009418:S100 Proteins
D002135:Calcium-Binding Proteins; D018797:Cell Cycle Proteins; D008081:Liposomes; D008565:Membrane Proteins; D010743:Phospholipids; D000075383:S100 Calcium Binding Protein A6; D009418:S100 Proteins; C489134:S100a6 protein, mouse; D004533:Egtazic Acid; D017830:Octoxynol; D002118:Calcium