Return to search

Studies on the Purification and Phosphorylation of Phosphofructokinase from Ascaris suum

A new procedure has been developed to concentrate the phosphofructokinase from muscle of Ascaris suum with minimum loss of activity. By utilizing this method, 50 ml fraction was concentrated to a final volume of 3 ml in about 1.5 h without loss in enzyme activity. The concentrated enzyme had a specific activity of 64 units per mg. Ascaris muscle-cuticle was incubated in 50 1M solutions of either acetylcholine, serotonin, y-aminobutyric acid, levamisole, or saline alone. Phosphate analysis of the isolated phosphofructokinase from each incubation revealed that the enzyme contained the following moles of phosphate per subunit: 2.9 (acetylcholine), 2.2 (serotonin), 2.0 (y-aminobutyric acid), 1.5 (levamisole), and 3.4 (salne alone). The present study did not establish a direct correlation between degree of phosphorylation and phosphofructokinase activity. Phosphofructokinase from muscle of Ascaris suum appears to contain several phosphorylation sites, and one of these sites is required to be phosphorylated in order for the enzyme to exhibit maximum activity under physiological conditions.

Identiferoai:union.ndltd.org:unt.edu/info:ark/67531/metadc503913
Date08 1900
CreatorsKaeini, Mohammad R. (Mohammad Reza)
ContributorsHarris, Ben G., Zimmerman, Earl G.
PublisherNorth Texas State University
Source SetsUniversity of North Texas
LanguageEnglish
Detected LanguageEnglish
TypeThesis or Dissertation
Formatv, 39 leaves: ill., Text
RightsPublic, Kaeini, Mohammad R. (Mohammad Reza), Copyright, Copyright is held by the author, unless otherwise noted. All rights reserved.

Page generated in 0.0018 seconds