PARTIAL PURIFICATION AND PROPERTIES OFANGIOTENSIN I CONVERTING ENZYME FROM RABBIT PLASMA
スポンサーリンク
概要
- 論文の詳細を見る
Angiotensin I converting enzyme was purified from rabbit plasma by means of ammonium sulfate fractionation, DEAE-Sephadex A-50 column chromatography and Sephadex G-200 gel filtration. The purified material was separated from angiotensinase, carboxypeptidase and L-leucyl-β-naphthylamidase, but could not be separated from di- or tri-peptidases. The specific activity of the enzyme was elevated 63 fold by the purification method. The purified material produced angiotensin II, His-Leu, histidine and leucine when incubated with angiotensin I at 37℃, pH 7.2 for 20 hours. This fact suggests that the enzyme hydrolyses the Phe-His bond of angiotensin I. The enzyme activity was inhibited by the addition of 10^<-3>M EDTA. Optimum pH of the enzyme was about pH 7.2.
- 社団法人日本循環器学会の論文
著者
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Kokubu Tatsuo
The Third Department Of Internal Medicine Osaka University Medical School
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Yamamura Yuichi
President of Osaka University
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Yamamura Yuichi
The Third Department of Internal Medicine, Osaka University Medical School
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Akutsu Hiroshi
3rd Dept. Of Intern. Med.. Osaka Univ. Med. School.
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Ueda Einosuke
The Second Department Of Internal Medicine Ehime University School Of Medicine
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Ueda Einosuke
The Third Department Of Internal Medicine Osaka University Medical School
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AKUTSU HIROSHI
The Third Department of Medicine. Osaha University Hospital
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Kokubu Tatsuo
3rd Dept. Of Intern. Med.. Osaka Univ. Med. School.
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Akutsu Hiroshi
The 3rd Department Of Medicine Osako University Medical Schcol
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Yamamura Yuichi
The Third Dept. Of Med. Osaka Univ. School Of Med.
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Kokubu Tatsijo
3rd Dept. Of Intern. Med.. Osaka Univ. Med. School.
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Yamamura Yuichi
Third Department Of Medicine Osaka University Hospital
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YAMAMURA YUICHI
The Third Department of Internal Medicine, Medical School of Osaka University
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