ENZYMATIC DECARBOXYLATION OF L-THREO-3, 4-DIHYDROXYPHENYLSERINE IN RAT HEART
スポンサーリンク
概要
- 論文の詳細を見る
Decarboxylation of L-threo-3, 4-dihydroxyphenylserine (L-threo-DOPS) by the higher speed supernatant of the rat heart homogenate and the regional distribution of L-threo-DOPS decarboxylase activity were examined. Decarboxylation was demonstrated to occur specifically with L-isomer but not with D-isomer. Addition of pyrogallol was necessary for maximal recovery of norepinephrine. The optimal condition for decarboxylation of L-threo-DOPS by the rat heart enzyme was similar to conditions required with the enzymes from brain and kidney. Under the optimal conditions, Km and Vmax for L-threo-DOPS were 2.1 mM and 6.4 nmoles/mg protein/15 min, respectively. Decarboxylation of L-threo-DOPS was markedly inhibited by D-threo-DOPS and D-DOPA. The L-aromatic amino acid decarboxylase activity was highest in the right auricle followed by the atrial body, the left auricle, the right ventricle and the left ventricle.
- 社団法人 日本薬理学会の論文
著者
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Inagaki Chiyoko
Department Of Biology Kyoto College Of Pharmacy
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Tanaka Chikako
Department Of Anesthesiology Keio University School Of Medicine
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ARAKI Hiromasa
Department of Pharmacology, Kobe University School of Medicine
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OHMURA Ippei
Department of Pharmacology, School of Medicine, Kobe University
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INAGAKI Chiyoko
Departmctit of Pharmacology, Faculty of Medicine, Kyoto University
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TANAKA Chikako
Department of Pharmacology, School of Medicine, Kobe University
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