A Common Phosphorylation Site for Cyclic AMP-dependent Protein Kinase and Protein Kinase C in Human Placental 6-Phosphofructo-2-kinase/Fructose-2,6-bisphosphatase
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概要
- 論文の詳細を見る
Human placental 6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase (HP2K) was phosphorylated by incubation with [γ-^<32> P] MgATP and cyclic AMP-dependent protein kinase (PKA) or protein kinase C (PKC). Approximately 0.8 mol of phosphate per mol subunit of HP2K was incorporated by either PKA or PKC. However, with additional incubation with PKA following incubation with PKC or vice versa, no additional phosphate was incorporated into the HP2K. The phosphorylation sites for the two protein kinases were identified by peptide mapping and microsequencing following digestion of phosphorylated-HP2K with clostripain. Evidence is also suggested for a common phosphorylation site (Ser-460) for PKA and PKC.
- 社団法人日本農芸化学会の論文
- 1998-10-23
著者
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Okamura Noriko
Department Of Clinical Pharmaceutics Graduate School Of Pharmaceutical Sciences Nagasaki University
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Okamura Noriko
Department Of Biochemistry School Of Pharmaceutical Sciences Nagasaki University
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Sakakibara Ryuzo
Laboratory Of Biochemistry Department Of Pharmacy Faculty Of Pharmaceutical Sciences Nagasaki Intern
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Sakakibara Ryuzo
Department Of Biochemistry School Of Clinical Pharmaceutical Science Nagasaki University
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