Cataract and the Acceleration of Calpain-Induced /?-Crystallin Insolubilization Occurring During Normal Maturation of Rat Lens
نویسندگان
چکیده
Methods. Soluble and insoluble lens proteins from 4-day-old to 4-month-old rat lens cortexes and nuclei were separated by two-dimensional electrophoresis. The insoluble proteins from 4-month-old nuclei were electroblotted and the NH2 termini of proteins sequenced. Cleavage sites appearing at 4 months of age were compared to cleavage sites produced by purified calpain II and to cleavage sites appearing in cataracts induced by selenite in vivo or in lenses cultured with calcium ionophore A23187 or diamide.
منابع مشابه
Cataract and the acceleration of calpain-induced beta-crystallin insolubilization occurring during normal maturation of rat lens.
PURPOSE To determine if limited proteolysis of beta-crystallins is associated with insolubilization of proteins in rats lens during maturation and to test if the protease, calpain II, is involved. METHODS Soluble and insoluble lens proteins from 4-day-old to 4-month-old rat lens cortexes and nuclei were separated by two-dimensional electrophoresis. The insoluble proteins from 4-month-old nucl...
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تاریخ انتشار 2005