Adenosine Triphosphate-Adenosine 5'-Monophosphate Phosphotransferase of Bovine Liver Mitochondria

Adenosine Triphosphate : Guanosine Monophosphate Phosphotransferase

Several laboratories have reported studies on individual enzymes that belong to the general class of adenosine triphosphate : nucleoside monophosphate phosphotransferases (EC 2.7.4.4), commonly termed nucleoside monophosphate kinases (l-7). Studies with partially purified enzyme preparations have indicated that a variety of nucleoside monophosphates can serve as alternative substrates for nucle...

Rat liver adenosine triphosphate: adenosine monophosphate phosphotransferase activity. II. Subcellular localization of adenylate kinase isozymes.

Adenylate kinase activity (ATP:AMP-phosphotransferase, EC 2.7.4.3) was studied in subcellular extracts of rat liver tissue. Essentially all of the activity, over 150 units per g of tissue, wet weight (1.7 units per mg of protein), was released into the cytosol when the tissue was homogenized in 0.025 M sucrose. Isotonic (0.25 M sucrose) homogenization and separation of subcellular fractions by ...

Adenosine triphosphate: adenosine monophosphate phosphotransferase isozymes in rat liver and hepatomas.

Activation of skeletal muscle phosphorylase kinase by adenosine triphosphate and adenosine 3',5'-monophosphate.

Rabbit skeletal muscle phosphorylase kinase has been obtained as a nearly homogeneous protein showing a single peak on electrophoresis and in the ultracentrifuge. Incubation of the purified kinase with T~~P-ATP in the presence of Mg++ ions activates the enzyme; this process is accompanied by phosphorylation of the protein. Activation and phosphorylation of phosphorylase kinase occur more rapidl...

Proton movements and adenosine triphosphate synthesis in rat liver mitochondria.

In a previous communication (Archbold et al., 1974) we have described experiments the results of which are not readily reconciled with some aspects of the chemiosmotic hypothesis. Our interpretation required a distinction between the distributive nature ofelectroneutral (EN) and eiectrogenic (EG) proton movements across the mitochondria1 inner membrane. This distinction has not been made hither...