Die Substratspezifität ,,anorganischer“ Poly- und Metaphosphatasen. II. Trennung der Enzyme
- 1 January 1956
- journal article
- research article
- Published by Walter de Gruyter GmbH in Hoppe-Seyler´s Zeitschrift Für Physiologische Chemie
- Vol. 303 (Jahresband), 115-124
- https://doi.org/10.1515/bchm2.1956.303.1-2.115
Abstract
Yeast maceration juice con-tains enzymes hydrolysing pyrophosphate, tri- and tetrapoly-phosphate, Graham''s salt, and tri- and tetrametaphosphate. Pyrophosphatase and tripolyphosphatase were separated from the other enzymes by precipitation at pH 4.1; these two enzymes were separated by paper electrophoresis. The enzyme hydrolyz-ing tetrapolyphosphate, tetrametaphosphate and Graham'' s salt were inactivated by "autoproteolysis"; they were distinguished by their relative adsorptions on alumina and on calcium bento-nite. The metaphosphatases were precipitated by between 20-40% saturated ammonium sulfate, while the polyphosphatases were precipitated by between 40 and 60%.This publication has 5 references indexed in Scilit:
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