Use of immobilized lactoperoxidase to label L cell proteins involved in adhesion to polystyrene.
Proteins involved in the attachment of murine L cells to polystyrene have been identified by a technique designed to iodinate only those macromolecules coming into closet apposition to the substratum. Whereas soluble lactoperoxidase (LPO) catalyzes the radioiodination of a broad spectrum of polypeptides, the same enzyme immobilized on polystyrene tissue culture flasks discriminately labels 55,000 and 42,000 mol wt polypeptides that adhere tightly to the substratum after the cells are removed. One-dimensional peptide mapping following limited proteolysis showed that the labeled 55,000 mol wt polypeptide is similar to a component of comparable molecular weight present in the detergent-extracted cytoskeleton. The functional association of two cytoskeletal structures, presumably 10-nm filaments and actin, is discussed, and alternative explanations for their susceptibility to iodination by immobilized LPO are presented.
D000199:Actins / Q000502:physiology*; D000818:Animals; D002448:Cell Adhesion; D003599:Cytoskeleton / Q000502:physiology; D004800:Enzymes, Immobilized; D007739:L Cells; D007784:Lactoperoxidase; D008565:Membrane Proteins / Q000032:analysis / Q000502:physiology*; D051379:Mice; D008970:Molecular Weight; D010455:Peptides / Q000032:analysis; D011137:Polystyrenes
D000199:Actins; D004800:Enzymes, Immobilized; D008565:Membrane Proteins; D010455:Peptides; D011137:Polystyrenes; D007784:Lactoperoxidase