Phosphatidyl inositol 4,5-bisphosphate-specific phospholipase C in bovine rod outer segment membranes
Polyphosphoinositide-specific phosphodiesterase (phospholipase C) activity against phosphatidylinositol 4,5-bisphosphate has been examined in disrupted bovine retinal rod outer segments. The enzyme was strictly modulated by free calcium ion concentration and maximally activated at 10(-5) M Ca2+ (91 +/- 4 nmoles phosphatidylinositol 4,5-bisphosphate hydrolyzed/min/mg of protein). Guanine nucleotides did not affect in vitro phospholipase C activity either in the presence or absence of light, carbachol or epinephrine. The pH optimum at 10(-5) M Ca2+ in the presence of sodium deoxycholate was 6.5. The enzyme of bovine rod outer segments was concluded to be indirectly regulated by the phototransduction events.
| Medienart: |
Artikel |
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| Erscheinungsjahr: |
1992 |
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| Erschienen: |
1992 |
| Enthalten in: |
Zur Gesamtaufnahme - volume:41 |
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| Enthalten in: |
The Italian journal of biochemistry - 41(1992), 1 vom: 13. Jan., Seite 16-25 |
| Sprache: |
Englisch |
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| Beteiligte Personen: |
Panfoli, I [VerfasserIn] |
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| Anmerkungen: |
Date Completed 21.07.1992 Date Revised 19.11.2015 published: Print Citation Status MEDLINE |
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| Förderinstitution / Projekttitel: |
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| PPN (Katalog-ID): |
NLM013000241 |
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| 245 | 1 | 0 | |a Phosphatidyl inositol 4,5-bisphosphate-specific phospholipase C in bovine rod outer segment membranes |
| 264 | 1 | |c 1992 | |
| 336 | |a Text |b txt |2 rdacontent | ||
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| 500 | |a Date Completed 21.07.1992 | ||
| 500 | |a Date Revised 19.11.2015 | ||
| 500 | |a published: Print | ||
| 500 | |a Citation Status MEDLINE | ||
| 520 | |a Polyphosphoinositide-specific phosphodiesterase (phospholipase C) activity against phosphatidylinositol 4,5-bisphosphate has been examined in disrupted bovine retinal rod outer segments. The enzyme was strictly modulated by free calcium ion concentration and maximally activated at 10(-5) M Ca2+ (91 +/- 4 nmoles phosphatidylinositol 4,5-bisphosphate hydrolyzed/min/mg of protein). Guanine nucleotides did not affect in vitro phospholipase C activity either in the presence or absence of light, carbachol or epinephrine. The pH optimum at 10(-5) M Ca2+ in the presence of sodium deoxycholate was 6.5. The enzyme of bovine rod outer segments was concluded to be indirectly regulated by the phototransduction events | ||
| 650 | 4 | |a Journal Article | |
| 650 | 4 | |a Research Support, Non-U.S. Gov't | |
| 650 | 7 | |a Guanine Nucleotides |2 NLM | |
| 650 | 7 | |a Phosphatidylinositol 4,5-Diphosphate |2 NLM | |
| 650 | 7 | |a Phosphatidylinositol Phosphates |2 NLM | |
| 650 | 7 | |a Carbachol |2 NLM | |
| 650 | 7 | |a 8Y164V895Y |2 NLM | |
| 650 | 7 | |a Type C Phospholipases |2 NLM | |
| 650 | 7 | |a EC 3.1.4.- |2 NLM | |
| 650 | 7 | |a Calcium |2 NLM | |
| 650 | 7 | |a SY7Q814VUP |2 NLM | |
| 650 | 7 | |a Epinephrine |2 NLM | |
| 650 | 7 | |a YKH834O4BH |2 NLM | |
| 700 | 1 | |a Morelli, A |e verfasserin |4 aut | |
| 700 | 1 | |a Pepe, I M |e verfasserin |4 aut | |
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