Two components of cysteine oxidase in rat liver |
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Authors: | Shigeki Sakakibara Kenji Yamaguchi Iwao Ueda Yukiya Sakamoto |
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Institution: | Department of Medical Chemistry, Osaka Medical College 2-7, Daigakucho, Takatsuki, Osaka, Japan;Institute of Cancer Research, Osaka University Medical School, Osaka, Japan |
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Abstract: | Purified cysteine oxidase in rat liver is composed of two distinct proteins. These proteins are able to be fractionated by DEAE-cellulose column chromatography. It appears that one of them is a catalytic protein named protein-B having tightly bound iron as a prosthetic group, while the other is either a modifier or activating protein named protein-A. Protein-B is found to exist in both an active and an inactive form. Inactive protein-B is activated by incubation with substrate cysteine under anaerobic condition. Activated protein-B alone exhibited an extremely low catalytic activity but in the presence of protein-A remarkable increase in activity was observed. |
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Keywords: | All correspondence should be addressed to this author |
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