Visualization of lactoperoxidase binding to microtubule and tubulin |
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| Authors: | T Suzuki T Fujii R Tanaka |
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| Institution: | 1. Division of Cardiac Surgery, University of Maryland Medical Center, 110 S. Paca Street, 7th Floor, 21201, Baltimore, MD, USA;2. Retina Specialty Institute, 6717 North 11th Place Suite C, 32605, Gainesville, FL, USA;1. Molecular and Cellular Cardiology, Department of Medicine, University of California, One Shields Avenue, 95616, Davis, CA, USA;2. Division of Cardiology, Department of Internal Medicine, Kangbuk Samsung Hospital, Sungkyunkwan University School of Medicine, Seoul, Republic of Korea;3. VA Medical Center, Sacramento, CA, USA;1. Key Laboratory of Carcinogenesis and Cancer Invasion, Ministry of Education, Liver Cancer Institute, Zhongshan Hospital, Fudan University, 136 Yi Xue Yuan Road, 200032, Shanghai, China |
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| Abstract: | 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. |
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