A calcium-protease activator associated with brain microsomal-insoluble elements |
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Authors: | Y Takeyama H Nakanishi Y Uratsuji A Kishimoto Y Nishizuka |
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Affiliation: | Department of Biochemistry, Kobe University School of Medicine, Kobe 650, Japan |
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Abstract: | A factor which markedly activates Ca2+-dependent thiol protease (calpain) is associated with Triton X-100-insoluble materials, presumably structural elements such as cytoskeletons, of bovine brain microsomal fraction. This factor is extracted with 0.6 M KC1, and purified partially by sucrose density gradient centrifugation and hydroxyapatite column chromatography. The factor appears to be a heat-stable protein with an approximate Mr of 15 000. With casein as substrate this factor activates both calpain I and calpain II several-fold up to more than 10- fold without alteration of their affinity to Ca2+. Calmodulin is unable to substitute for this factor. A similar factor is associated with human platelet insoluble materials. |
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