Purification and Characterization of Endogenous Protein Activator of Human Platelet Proteasome
An endogenous activator of 20S proteasome was purified from human platelets and its effect on three peptidase activities of proteasome was studied. This activator had a molecular weight of 170 kDa, and was composed of 32 kDa polypeptides as determined by SDS-PAGE. It was highly labile upon heat trea...
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Veröffentlicht in: | Journal of biochemistry (Tokyo) 1993-09, Vol.114 (3), p.317-323 |
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Format: | Artikel |
Sprache: | eng |
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