Metabolism and certain properties of the proteinase that controls catalase metabolism in rat liver mitochondria
A Mg, ATP-dependent serine proteinase with a molecular weight of 50 kD and optimum action at pH 8.0 was isolated and purified 750-fold. The substrate specificity was studied for a series of protein substrates: catalase, aldolase, urate oxidase, superoxide dismutase, albumin, cytochrome c, and insuli...
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Veröffentlicht in: | Biochemistry (Easton) 1988-01, Vol.52 (7), p.930-935 |
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Hauptverfasser: | , |
Format: | Artikel |
Sprache: | eng |
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Online-Zugang: | Volltext |
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Zusammenfassung: | A Mg, ATP-dependent serine proteinase with a molecular weight of 50 kD and optimum action at pH 8.0 was isolated and purified 750-fold. The substrate specificity was studied for a series of protein substrates: catalase, aldolase, urate oxidase, superoxide dismutase, albumin, cytochrome c, and insulin. It was shown that the proteinase possesses affinity for proteins with molecular weight above 100 kD. The quantitative characteristics of its metabolism were studied. |
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ISSN: | 0006-2960 |