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ID 32055
JaLCDOI
フルテキストURL
著者
Tsutsui, Ken Okayama University
Hatase, Osamu Okayama University
Oda, Takuzo Okayama University
抄録

Catalase was partially purified (about 380-fold purification) from the post-mitochondrial supernatant of bovine heart and compared with catalases from bovine erythrocytes and bovine liver. The electrophoretic mobility in polyacrylamide gel (pH 8.0) of heart catalase was the same as that of erythrocyte catalase and was smaller than that of the liver enzyme. The heart catalase was indistinguishable from erythrocyte catalase in regard to the molecular weights of subunit polypeptides, the inhibition patterns produced by several catalase inhibitors, and specific activity. The pH-activity curve of heart catalase consisted of a characteristic biphasic pattern with a peak at pH 7.5 and a shoulder at pH 10.

キーワード
catalse
muscle
bovine heart
Amo Type
Article
発行日
1979-04
出版物タイトル
Acta Medica Okayama
33巻
2号
出版者
Okayama University Medical School
開始ページ
103
終了ページ
111
ISSN
0386-300X
NCID
AA00508441
資料タイプ
学術雑誌論文
言語
English
論文のバージョン
publisher
査読
有り
PubMed ID
NAID