Soluble and Particulate Porphobilinogen-Deaminase from Dark-Grown Euglena gracilis

A highly efficient method employing NaSCN as a chaotropic agent was used to dissociate the membrane-bound porphobilinogen-deaminase. The same sequence of steps was applied for purifying both soluble and membrane dissociated porphobilinogen-deam inase. The chromatographic behaviour of both proteins w...

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Veröffentlicht in:Zeitschrift für Naturforschung C. A journal of biosciences 1989-08, Vol.44 (7), p.578-580
Hauptverfasser: Rossetti, M. V., Juknat, A. A., Batlle, A. M. del C.
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container_title Zeitschrift für Naturforschung C. A journal of biosciences
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creator Rossetti, M. V.
Juknat, A. A.
Batlle, A. M. del C.
description A highly efficient method employing NaSCN as a chaotropic agent was used to dissociate the membrane-bound porphobilinogen-deaminase. The same sequence of steps was applied for purifying both soluble and membrane dissociated porphobilinogen-deam inase. The chromatographic behaviour of both proteins was quite similar. Euglena gracilis deam inase appears to exist in an equilibrium mixture of two active species of relative molecular masses of 40000 and 20000.
doi_str_mv 10.1515/znc-1989-7-807
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source Elektronische Zeitschriftenbibliothek - Frei zugängliche E-Journals
subjects chromatography
Euglena gracilis
membrane proteins
Particulate
Porphobilinogen-Deaminase
Porphyrins
Soluble
title Soluble and Particulate Porphobilinogen-Deaminase from Dark-Grown Euglena gracilis
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