Exopeptidases of Clostridium histolyticum

A group of enzymes, fractionally precipitated from Cl. histolyticum filtrates at high ammonium sulfate concentrations, was found capable of hydrolyzing a wide variety of simple peptide substrates. The peptidases have been characterized; their pH optima, stability, behavior toward metal ions and vari... Ausführliche Beschreibung

1. Person: Mandl, I.
Weitere Personen: Ferguson, L.T.; Zaffuto, S.F.
Quelle: in Archives of Biochemistry and Biophysics Vol. 69 (1957), p. 565-581
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Format: Online-Artikel
Sprache: English
Veröffentlicht: 1957
Beschreibung: Online-Ressource
Online Zugang: Online
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Anmerkung: Copyright: Copyright (c) 2005 Elsevier (USA)
Zusammenfassung: A group of enzymes, fractionally precipitated from Cl. histolyticum filtrates at high ammonium sulfate concentrations, was found capable of hydrolyzing a wide variety of simple peptide substrates. The peptidases have been characterized; their pH optima, stability, behavior toward metal ions and various inhibitors, kinetics, and specificity were studied and comparisons were made with other known exopeptidases. It was found that a number of different enzymes was involved and that their ratio varied considerably in different preparations. The enzymes are not identical with any known group, including previously reported Cl. histolyticum enzymes.
ISSN: 0003-9861

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