Adenosine Triphosphatase in Isolated Membranes of Staphylococcus aureus
AUTOR(ES)
Gross, R.
RESUMO
The preparation of cytoplasmic membranes from suspensions of Staphylococcus aureus lysed by an enzyme recently isolated in these laboratories is described. These membranes contained: protein, 34.4%; ribonucleic acid, 6.6%; lipids, 34.5%; and total phosphorus, 1.4%. Such membranes exhibited adenosine 5′-triphosphatase (E.C. 3.6.1.3) activity, liberating orthophosphate at an initial rate of 0.53 μmole per min per mg of protein under optimal conditions. The enzyme was Mg++-dependent and K+- or Na+-stimulated. Maximal activity was observed with a molar adenosine 5′-triphosphate (ATP) to Mg++ ratio of 1. One mole of orthophosphate was liberated per mole of ATP; the other product of digestion was adenosine 5′-diphosphate. Inorganic pyrophosphate and the 5′-triphosphates of guanosine, uridine, and cytidine were also attacked by membrane preparations, but more slowly than ATP. Ouabain, p-chloromercuribenzoate, and 2,4-dinitrophenol did not alter adenosine triphosphatase activity, whereas both Atebrine and chlorpromazine were inhibitory.
ACESSO AO ARTIGO
http://www.pubmedcentral.nih.gov/articlerender.fcgi?artid=315089Documentos Relacionados
- Staphylococcus aureus adenosine triphosphatase: inhibitor sensitivity and release from membrane.
- Adenosine Triphosphatase Activity of Mycoplasma Membranes1
- Effects of Germination on NA+-K+-stimulated Adenosine 5′-Triphosphatase and ATP-dependent Ion Transport of Isolated Membranes from Cotyledons
- Solubilization of adenosine triphosphatase from membranes of Escherichia coli: effect of p-aminobenzamidine.
- Characterization of the H+ Translocating Adenosine Triphosphatase and Pyrophosphatase of Vacuolar Membranes Isolated by Means of a Perfusion Technique from Chara corallina1