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Characterization of <em>N</em>ω-phosphoarginine hydrolase from rat liver.
- Source :
- European Journal of Biochemistry; 9/15/92, Vol. 208 Issue 3, p747-752, 6p
- Publication Year :
- 1992
-
Abstract
- N<superscript>ω</superscript>-Phosphoarginine hydrolase from rat liver hydrolyzed N<superscript>ω</superscript>-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<superscript>ω</superscript>-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) 9-1auryl 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 μM and 12 μM, respectively; some proteins stimulated the activity, while lysophosphatidic acid, lysophosphatidylinositol, and phosphatidic acid suppressed the activity even in the presence of poly(oxyethylene) 9-1auryl ether. [ABSTRACT FROM AUTHOR]
- Subjects :
- ALKALI metals
SODIUM
LYSOPHOSPHOLIPIDS
PROTEINS
AMINO acids
PHOSPHORYLATION
Subjects
Details
- Language :
- English
- ISSN :
- 00142956
- Volume :
- 208
- Issue :
- 3
- Database :
- Complementary Index
- Journal :
- European Journal of Biochemistry
- Publication Type :
- Academic Journal
- Accession number :
- 13684285
- Full Text :
- https://doi.org/10.1111/j.1432-1033.1992.tb17243.x