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Phosphorylation of pig brain diacylglycerol kinase by endogenous protein kinase
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| Zeitschriftentitel: | FEBS Letters |
|---|---|
| Personen und Körperschaften: | , |
| In: | FEBS Letters, 201, 1986, 1, S. 97-100 |
| Format: | E-Article |
| Sprache: | Englisch |
| veröffentlicht: |
Wiley
|
| Schlagwörter: |
| author_facet |
Kanoh, Hideo Ono, Teruo Kanoh, Hideo Ono, Teruo |
|---|---|
| author |
Kanoh, Hideo Ono, Teruo |
| spellingShingle |
Kanoh, Hideo Ono, Teruo FEBS Letters Phosphorylation of pig brain diacylglycerol kinase by endogenous protein kinase Cell Biology Genetics Molecular Biology Biochemistry Structural Biology Biophysics |
| author_sort |
kanoh, hideo |
| spelling |
Kanoh, Hideo Ono, Teruo 0014-5793 1873-3468 Wiley Cell Biology Genetics Molecular Biology Biochemistry Structural Biology Biophysics http://dx.doi.org/10.1016/0014-5793(86)80577-4 <jats:p>Pig brain diacylglycerol kinase did not catalyze autophosphorylation. However, the kinase was phosphorylated on serine, when immunoprecipitated from the partially purified enzyme preparation preincubated with Mg<jats:sup>2+</jats:sup> and [γ‐<jats:sup>32</jats:sup>P]ATP. The action of the endogenous protein kinase phosphorylating diacylglycerol kinase was independent of cyclic nucleotides and Ca<jats:sup>2+</jats:sup>, and became maximum at pH 5.5. Although the extent of enzyme phosphorylation was limited (maximally about 0.25 mol P<jats:sub>i</jats:sub> incorporated per mol kinase), the results show that diacylglycerol kinase can be a phosphoprotein.</jats:p> Phosphorylation of pig brain diacylglycerol kinase by endogenous protein kinase FEBS Letters |
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10.1016/0014-5793(86)80577-4 |
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Wiley, 1986 |
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Wiley, 1986 |
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1873-3468 0014-5793 |
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1986 |
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Wiley |
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FEBS Letters |
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49 |
| title |
Phosphorylation of pig brain diacylglycerol kinase by endogenous protein kinase |
| title_unstemmed |
Phosphorylation of pig brain diacylglycerol kinase by endogenous protein kinase |
| title_full |
Phosphorylation of pig brain diacylglycerol kinase by endogenous protein kinase |
| title_fullStr |
Phosphorylation of pig brain diacylglycerol kinase by endogenous protein kinase |
| title_full_unstemmed |
Phosphorylation of pig brain diacylglycerol kinase by endogenous protein kinase |
| title_short |
Phosphorylation of pig brain diacylglycerol kinase by endogenous protein kinase |
| title_sort |
phosphorylation of pig brain diacylglycerol kinase by endogenous protein kinase |
| topic |
Cell Biology Genetics Molecular Biology Biochemistry Structural Biology Biophysics |
| url |
http://dx.doi.org/10.1016/0014-5793(86)80577-4 |
| publishDate |
1986 |
| physical |
97-100 |
| description |
<jats:p>Pig brain diacylglycerol kinase did not catalyze autophosphorylation. However, the kinase was phosphorylated on serine, when immunoprecipitated from the partially purified enzyme preparation preincubated with Mg<jats:sup>2+</jats:sup> and [γ‐<jats:sup>32</jats:sup>P]ATP. The action of the endogenous protein kinase phosphorylating diacylglycerol kinase was independent of cyclic nucleotides and Ca<jats:sup>2+</jats:sup>, and became maximum at pH 5.5. Although the extent of enzyme phosphorylation was limited (maximally about 0.25 mol P<jats:sub>i</jats:sub> incorporated per mol kinase), the results show that diacylglycerol kinase can be a phosphoprotein.</jats:p> |
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| author | Kanoh, Hideo, Ono, Teruo |
| author_facet | Kanoh, Hideo, Ono, Teruo, Kanoh, Hideo, Ono, Teruo |
| author_sort | kanoh, hideo |
| container_issue | 1 |
| container_start_page | 97 |
| container_title | FEBS Letters |
| container_volume | 201 |
| description | <jats:p>Pig brain diacylglycerol kinase did not catalyze autophosphorylation. However, the kinase was phosphorylated on serine, when immunoprecipitated from the partially purified enzyme preparation preincubated with Mg<jats:sup>2+</jats:sup> and [γ‐<jats:sup>32</jats:sup>P]ATP. The action of the endogenous protein kinase phosphorylating diacylglycerol kinase was independent of cyclic nucleotides and Ca<jats:sup>2+</jats:sup>, and became maximum at pH 5.5. Although the extent of enzyme phosphorylation was limited (maximally about 0.25 mol P<jats:sub>i</jats:sub> incorporated per mol kinase), the results show that diacylglycerol kinase can be a phosphoprotein.</jats:p> |
| doi_str_mv | 10.1016/0014-5793(86)80577-4 |
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| id | ai-49-aHR0cDovL2R4LmRvaS5vcmcvMTAuMTAxNi8wMDE0LTU3OTMoODYpODA1NzctNA |
| imprint | Wiley, 1986 |
| imprint_str_mv | Wiley, 1986 |
| institution | DE-D275, DE-Bn3, DE-Brt1, DE-Zwi2, DE-D161, DE-Zi4, DE-Gla1, DE-15, DE-Pl11, DE-Rs1, DE-14, DE-105, DE-Ch1, DE-L229 |
| issn | 1873-3468, 0014-5793 |
| issn_str_mv | 1873-3468, 0014-5793 |
| language | English |
| last_indexed | 2024-03-01T14:58:55.054Z |
| match_str | kanoh1986phosphorylationofpigbraindiacylglycerolkinasebyendogenousproteinkinase |
| mega_collection | Wiley (CrossRef) |
| physical | 97-100 |
| publishDate | 1986 |
| publishDateSort | 1986 |
| publisher | Wiley |
| record_format | ai |
| recordtype | ai |
| series | FEBS Letters |
| source_id | 49 |
| spelling | Kanoh, Hideo Ono, Teruo 0014-5793 1873-3468 Wiley Cell Biology Genetics Molecular Biology Biochemistry Structural Biology Biophysics http://dx.doi.org/10.1016/0014-5793(86)80577-4 <jats:p>Pig brain diacylglycerol kinase did not catalyze autophosphorylation. However, the kinase was phosphorylated on serine, when immunoprecipitated from the partially purified enzyme preparation preincubated with Mg<jats:sup>2+</jats:sup> and [γ‐<jats:sup>32</jats:sup>P]ATP. The action of the endogenous protein kinase phosphorylating diacylglycerol kinase was independent of cyclic nucleotides and Ca<jats:sup>2+</jats:sup>, and became maximum at pH 5.5. Although the extent of enzyme phosphorylation was limited (maximally about 0.25 mol P<jats:sub>i</jats:sub> incorporated per mol kinase), the results show that diacylglycerol kinase can be a phosphoprotein.</jats:p> Phosphorylation of pig brain diacylglycerol kinase by endogenous protein kinase FEBS Letters |
| spellingShingle | Kanoh, Hideo, Ono, Teruo, FEBS Letters, Phosphorylation of pig brain diacylglycerol kinase by endogenous protein kinase, Cell Biology, Genetics, Molecular Biology, Biochemistry, Structural Biology, Biophysics |
| title | Phosphorylation of pig brain diacylglycerol kinase by endogenous protein kinase |
| title_full | Phosphorylation of pig brain diacylglycerol kinase by endogenous protein kinase |
| title_fullStr | Phosphorylation of pig brain diacylglycerol kinase by endogenous protein kinase |
| title_full_unstemmed | Phosphorylation of pig brain diacylglycerol kinase by endogenous protein kinase |
| title_short | Phosphorylation of pig brain diacylglycerol kinase by endogenous protein kinase |
| title_sort | phosphorylation of pig brain diacylglycerol kinase by endogenous protein kinase |
| title_unstemmed | Phosphorylation of pig brain diacylglycerol kinase by endogenous protein kinase |
| topic | Cell Biology, Genetics, Molecular Biology, Biochemistry, Structural Biology, Biophysics |
| url | http://dx.doi.org/10.1016/0014-5793(86)80577-4 |