Beitrag zum Aktivierungsmechanismus der Phosphatasen. (Pyrophosphatase. II.)

  title={Beitrag zum Aktivierungsmechanismus der Phosphatasen. (Pyrophosphatase. II.)},
  author={Erwin K. Bauer},
  journal={Biological Chemistry},
  • E. Bauer
  • Published 1937
  • Biology
  • Biological Chemistry
12 Citations
Aktivierung einer alkalischen Phosphatase
β-Glycerophosphatase prepared from the intestinal mucosa of the calf was purified by fractionated precipitation with alcohol. A further concentration of the enzyme activity was attained by
Isolation of the inorganic pyrophosphatase from brewer's yeast and studies on the localization of this enzyme in brewer's and baker's yeast.
This data indicates that extensive purification of brewer's yeast pyrophosphatase results in the separation of three active forms of the enzyme, which is mainly located in the hyaloplasm for both brewer's and baker's yeast.
A kinetic model for the action of the inorganic pyrophosphatase from bakers' yeast. The activating influence of magnesium ions.
A systematic analysis of the kinetics of the crystallized inorganic pyrophosphatase from bakers' yeast is presented and it has been shown that from the two possible species of the 1:1 complex at pH 7.2 either the unprotonated form is the true substrate or the un Protonated and protonated forms together are alternative substrates.
20 Inorganic Pyrophosphatase of Escherichia coli
Publisher Summary This chapter discusses the molecular properties and catalytic properties of inorganic pyrophosphatase of Escherichia coli. Only a limited amount of information about the active site
  • T. Ricketts
  • Chemistry, Medicine
    Archives of biochemistry and biophysics
  • 1965
In its lack of inhibition by iodoacetate and its higher pH optimum, the inorganic pyrophosphatase resembled the firefly enzyme more closely than the enzymes of mammalian erythrocyte and brain, or yeast, although all the enzymes showed many points of similarity.
On the mechanism of metal activation of deoxyribobuclease I.
  • J. Wiberg
  • Chemistry, Medicine
    Archives of biochemistry and biophysics
  • 1958
In a study of activation by pairs of these metals, Ca ++ was found to be a potent Synergist in the Mg-activated reaction, increasing the maximum rate more than threefold, to give a rate comparable to that given by Mn ++ alone.
The magnesium activation of pyrophosphatase.
Evidence is presented that the activation of rat brain pyrophosphatase by Mg++ can be ascribed to a requirement of the enzyme for magnesium pyroph phosphate for a substrate.
Phosphatases of the liver. III. "Neutral" pyrophosphatase.
  • M. Swanson
  • Chemistry, Medicine
    The Journal of biological chemistry
  • 1952