دورية أكاديمية
Characterisation of nitric oxide synthase activity in the tropical sea anemone Aiptasia pallida.
| العنوان: | Characterisation of nitric oxide synthase activity in the tropical sea anemone Aiptasia pallida. |
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| المؤلفون: | Morrall CE; Plymouth Environmental Research Centre, University of Plymouth, UK. cmorrall@bbsr.edu, Galloway TS, Trapido-Rosenthal HG, Depledge MH |
| المصدر: | Comparative biochemistry and physiology. Part B, Biochemistry & molecular biology [Comp Biochem Physiol B Biochem Mol Biol] 2000 Apr; Vol. 125 (4), pp. 483-91. |
| نوع المنشور: | Journal Article; Research Support, Non-U.S. Gov't |
| اللغة: | English |
| بيانات الدورية: | Publisher: Pergamon Country of Publication: England NLM ID: 9516061 Publication Model: Print Cited Medium: Print ISSN: 1096-4959 (Print) Linking ISSN: 10964959 NLM ISO Abbreviation: Comp Biochem Physiol B Biochem Mol Biol Subsets: MEDLINE |
| أسماء مطبوعة: | Publication: Oxford : Pergamon Original Publication: Oxford : Tarrytown, NY : Pergamon ; Elsevier, c1994- |
| مواضيع طبية MeSH: | Nitric Oxide Synthase/*metabolism , Sea Anemones/*enzymology, Animals ; Arginine/analogs & derivatives ; Arginine/pharmacology ; Citrulline/analysis ; Citrulline/metabolism ; Enzyme Inhibitors/pharmacology ; Epithelial Cells/enzymology ; NADP/metabolism ; NADPH Dehydrogenase/analysis ; NADPH Dehydrogenase/metabolism ; NG-Nitroarginine Methyl Ester/pharmacology ; Nitric Oxide Synthase/antagonists & inhibitors ; Sea Anemones/physiology ; Staining and Labeling/methods ; Valine/pharmacology |
| مستخلص: | The presence of nitric oxide synthase (EC 1.14.23 NOS) activity is demonstrated in the tropical marine cnidarian Aiptasia pallida (Verrill). Enzyme activity was assayed by measuring the conversion of [3H]arginine to [3H]citrulline. Optimal NOS activity was found to require NADPH. Activity was inhibited by the competitive NOS inhibitor NG-methyl-L-arginine (L-NMA), but not the arginase inhibitors L-valine and L-ornithine. NOS activity was predominantly cytosolic, and was characterised by a Km for arginine of 19.05 microM and a Vmax of 2.96 pmol/min per microgram protein. Histochemical localisation of NOS activity using NADPH diaphorase staining showed the enzyme to be predominantly present in the epidermal cells and at the extremities of the mesoglea. These results provide a preliminary biochemical characterisation and histochemical localisation of NOS activity in A. pallida, an ecologically important sentinel species in tropical marine ecosystems. |
| المشرفين على المادة: | 0 (Enzyme Inhibitors) 0 (N(G)-monomethylarginine acetate) 29VT07BGDA (Citrulline) 53-59-8 (NADP) 94ZLA3W45F (Arginine) EC 1.14.13.39 (Nitric Oxide Synthase) EC 1.6.99.1 (NADPH Dehydrogenase) HG18B9YRS7 (Valine) V55S2QJN2X (NG-Nitroarginine Methyl Ester) |
| تواريخ الأحداث: | Date Created: 20000725 Date Completed: 20001124 Latest Revision: 20190915 |
| رمز التحديث: | 20231215 |
| DOI: | 10.1016/s0305-0491(00)00157-7 |
| PMID: | 10904861 |
| قاعدة البيانات: | MEDLINE |
Full Text Finder | تدمد: | 1096-4959 |
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| DOI: | 10.1016/s0305-0491(00)00157-7 |