Visualization of lactoperoxidase binding to microtubule and tubulin.
The binding of lactoperoxidase to microtubules and tubulin was shown in both electron micrography and polyacrylamide gel electrophoresis by tracing the enzymatic activity of lactoperoxidase. Lactoperoxidase bound to purified microtubules appeared to distribute evenly on the surface without forming special structures. Both alpha and beta-tubulin separated by sodium dodecylsulfate-polyacrylamide gel electrophoresis bound lactoperoxidase, and could be detected by the use of lactoperoxidase reaction. Electrophoretic study revealed that the interaction between lactoperoxidase and tubulin were not strictly specific and a variety of proteins other than alpha- and beta-tubulin, including actin and neurofilament subunits, bound lactoperoxidase.
D000818:Animals; D001921:Brain / Q000378:metabolism; D004591:Electrophoresis, Polyacrylamide Gel; D066298:In Vitro Techniques; D007784:Lactoperoxidase / Q000378:metabolism*; D008854:Microscopy, Electron; D008870:Microtubules / Q000378:metabolism*; D010544:Peroxidases / Q000378:metabolism*; D011485:Protein Binding; D011817:Rabbits; D051381:Rats; D013552:Swine; D014404:Tubulin / Q000378:metabolism*
D014404:Tubulin; D007784:Lactoperoxidase; D010544:Peroxidases