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Hemoproteins of Wheat Germ:III. Further Studies on Purification of Peroxidase and Some of Their Properties
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- SHIN MASATERU
- Department of Biology, Faculty of Science, University of Osaka
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- NAKAMURA WATARU
- Department of Biology, Faculty of Science, University of Osaka
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Description
1. An improved method was devised for purification of peroxidase 556 and peroxidase 566 from wheat germ. These peroxidases were obtained as crystals. Their homogeneity was shown by the migration hehavior on the resin and by the ultracentrifugal behavior.<br> 2. Peroxidase 566 was found to be a new type of peroxidases. Its absorption spectrum resembled that of b-cytochromes. Modified forms of peroxidase 566 had the absorption spectra similar to some peroxidases obtained by other investigators.<br> 3. Although the peroxidases had proto-heme as their prosthetic group, it was suggested from their molecular weights and other properties that properties of protein portions differ distinctly from each other.<br> The authors express their many thanks to Prof. Okunuki, K. for his guidance and encouragement during the work and to Dr. Kakiuchi, K. and Dr. Takagi, T. for their technical guidance in the ultracentrifugal and the diffusion analysis.
Journal
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- J Biochem (Tokyo)
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J Biochem (Tokyo) 50 (6), 500-507, 1961
The Japanese Biochemical Society
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Details 詳細情報について
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- CRID
- 1570572703174332160
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- NII Article ID
- 130003536776
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- ISSN
- 0021924X
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- Text Lang
- en
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- Data Source
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- CiNii Articles