Characterization of Nomega-phosphoarginine hydrolase from rat liver
- 1 September 1992
- journal article
- Published by Wiley in JBIC Journal of Biological Inorganic Chemistry
- Vol. 208 (3), 747-752
- https://doi.org/10.1111/j.1432-1033.1992.tb17243.x
Abstract
N omega-Phosphoarginine hydrolase from rat liver hydrolyzed N omega-phosphoarginine into arginine and inorganic phosphate, whereas it did not release inorganic phosphate from 19 other phosphorylated compounds containing a N-P bond, an O-P bond or a C-P bond. In addition, it was not able to transfer the phosphoryl moiety from N omega-phosphoarginine to ADP. These results indicated that this enzyme was distinct from both phosphoamidase and arginine kinase. Its properties were as follows: thiol compounds were essential for its activity; it was stimulated by 1.5-2-fold in the presence of 0.001% Lubrol, Tween 20, poly(oxyethylene) 9-lauryl ether and Nonidet P-40, while 0.004% sodium lauryl sulfate inhibited the activity completely; concentrations of sodium molybdate and sodium vanadate necessary for 50% inhibition were 7 microM and 12 microM, respectively; some proteins stimulated the activity, while lysophosphatidic acid, lysophosphatidylinositol, and phosphatidic acid suppressed the activity even in the presence of poly(oxyethylene) 9-lauryl ether.Keywords
This publication has 26 references indexed in Scilit:
- Characterization of a bovine brain magnesium-dependent phosphotyrosine protein phosphatase that is inhibited by micromolar concentrations of calciumBiochemical and Biophysical Research Communications, 1990
- The Structure And Regulation Of Protein PhosphatasesAnnual Review of Biochemistry, 1989
- Purification and physicochemical characterization of a human placental acid phosphatase possessing phosphotyrosyl protein phosphatase activityBiochemistry, 1988
- Characterization of an arginine‐specific protein kinase tightly bound to rat liver DNAJBIC Journal of Biological Inorganic Chemistry, 1987
- Isolation and purification of a new 105 kDa protein kinase from rat liver nucleiBiochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology, 1982
- Phosphorylation on basic amino acids in myelin basic proteinBiochemical and Biophysical Research Communications, 1976
- A Rapid and Sensitive Method for the Quantitation of Microgram Quantities of Protein Utilizing the Principle of Protein-Dye BindingAnalytical Biochemistry, 1976
- Determination of phosphate in serum and urine by a single step malachite-green methodClinica Chimica Acta; International Journal of Clinical Chemistry, 1975
- Phosphoramidates. V. Probable identity of rat liver microsomal glucose 6-phosphatase, phosphoramidase, and phosphoramidate-hexose phosphotransferaseBiochemistry, 1969
- Isolation ofBiochimica et Biophysica Acta (BBA) - General Subjects, 1967