Characterization of "abp38" in cytoskeleton of mouse myeloid leukemia cells and distribution of abp38 in various tissues.

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  • TAKAGI Kuniaki
    Department of Cytochemistry, Chest Disease Research Institute; Kyoto University|Department of Environmental Biochemistry, Shizuoka College of Pharmacy
  • ZENITA Koichi
    Department of Clinical Science, Faculty of Medicine, Kyoto University
  • ICHIKAWA Yasuo
    Department of Cytochemistry, Chest Disease Research Institute; Kyoto University

説明

A specific antibody was prepared against “abp38, ” a 38 kDa-dimer protein purified from mouse myeloid leukemia cells (M 1 cells), that induce gelation of actin filaments in a K+-dependent manner. Immunochemically, the total content of abp 38 in undifferentiated M 1 cells was found to be 0.89% of the total protein (10.7 μg/107 cells). This content increased about 8-fold (89.5 μg/107 cells) after the M 1 cells had differentiated into macrophages. When the cells before differentiation were extracted with Triton solution containing 150mM KCl, almost all abp38 in the cytoskeleton was removed, whereas in cells after differentiation, amount of abp38 remaining in the cytoskeleton was 4.5 μg per 107 cells. The amount of cytoskeleton-bound abp38 of M 1 cells and mouse peritoneal macrophages decreased with increase in K+ concentration in the extraction solution. Immunoreactive molecules against abp38 antibody were present in various tissues and cultured cell lines except for skeletal muscle and erythrocytes. Furthermore, actin binding protein with a molecular size of 38 kDa was found in bovine brain. These data suggest that abp38 is a ubiquitous protein present in various tissues and species.

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