Light-induced proteolysis of myosin heavy chain by Rose Bengal-conjugated antibody complexes.
Light-induced proteolysis of myosin heavy chain by Rose Bengal-conjugated antibody complexes.
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DOI：
10.1016/s1011-1344(01)00241-x
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发表时间：
2001-12
期刊：
影响因子：
--
通讯作者：
K. Conlon;M. Berrios
中科院分区：
文献类型：
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作者：
K. Conlon;M. Berrios
本文报道了氧杂蒽染料偶联抗体对鸡骨骼肌肌球蛋白重链的特异性光诱导非酶消化。将咕吨染料虎红与小鼠单克隆抗肌球蛋白一级特异性抗体或山羊抗小鼠IgG二级抗体偶联。在我们的实验条件下，当鸡骨骼肌肌球蛋白直接与虎红偶联抗肌球蛋白抗体形成复合物或间接与抗肌球蛋白抗体-虎红偶联二抗形成复合物时，可见光诱导肌球蛋白重链的非酶促分解。光化学反应的速率取决于照射时间和温度。虽然SDS-PAGE和免疫印迹分析表明，迁移到肌球蛋白重链多肽下方的片段占主导地位，但这些分析也表明产生了更高分子量的多肽。
The specific light-induced, non-enzymatic digestion of chicken skeletal muscle myosin heavy chain by xanthene dye-conjugated antibodies is reported. The xanthene dye Rose Bengal was conjugated to either a mouse monoclonal anti-myosin primary specific antibody or to goat anti-mouse IgG secondary antibodies. Under our experimental conditions, visible light induced the non-enzymatic breakdown of myosin heavy chains when chicken skeletal muscle myosin either directly formed a complex with Rose Bengal-conjugated anti-myosin antibodies or indirectly formed a complex with anti-myosin antibody-Rose Bengal-conjugated secondary antibodies. The rate of the photochemical reaction depended on irradiation time and temperature. Although SDS–PAGE and immunoblot analyses showed that fragments migrating below the myosin heavy chain polypeptide predominated, these analyses also showed higher molecular mass polypeptides were generated.