HYDROLYTIC DEACTIVATION OF KYOTORPHIN BY THE RODENT BRAIN HOMOGENATES AND SERA
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概要
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A simple analytica assay method for kyotorphin was developed by the use of amino acid analyzer and the deactivation of kyotorphin in biological media was studied with this method. Kyotorphin was hydrolyzed rapidly by enzymes in serum and brain of rat and mouse, but L-tyrosyl-D-arginine was not. The hydrolysis activity was much higher in brain than in serum. The apparent Michaelis' constants, K_m, were of the order of 10^<-5> M for brain and 10^<-4> M for serum in both species. The hydrolysis of kyotorphin was strongly inhibited by bestatin (K_i = 0.1μM). Thus the hydrolysis might be attributed to aminopeptidase(s). A dose of 50 μg of bestatin administered intracisternally potentiated the analgesic activity of kyotorphin by 4.8 times or so. Thus kyotorphin seems to be deactivated by bestatin-sensitive aminopeptidase (s) in brain.
- 公益社団法人日本薬学会の論文
著者
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TAKAGI Hiroshi
Department of Surgery II, University School of Medicine
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ONO Kenji
Forestry and Forest Product Research Institute
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Takagi Hiroshi
Department Of Medicine And Molecular Science Gunma University Graduate School Of Medicine
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TAKEGOSHI TOSHIO
Research Institute, Daiichi Seiyaku Co., Ltd.
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Takagi Hiroshi
Department Of Bioscience Fukui Prefectural University
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Takegoshi Toshio
Research Institute Daiichi Seiyaku Co. Ltd.
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Takagi Hiroshi
Department Of Bioscience Faculty Of Bioscience Fukui Prefectural University
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