Polymorphism of acid and neutral .ALPHA.-glucosidases in banana pulp:Changes in apparent pIs and affinity to Con A of the enzymes during ripening.
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- KONISHI Yôtarô
- Department of Food and Nutrition, Faculty of Science of Living, Osaka City University
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- KITAZATO Sachiko
- Department of Food and Nutrition, Faculty of Science of Living, Osaka City University
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- ASANO Ryôko
- Department of Food and Nutrition, Faculty of Science of Living, Osaka City University
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- NAKATANI Nobuji
- Department of Food and Nutrition, Faculty of Science of Living, Osaka City University
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We observed the presence of acid and neutral α-glucosidases with optimum pHs of 4.5 and 6.5, respectively, and their multiple forms in banana pulp. By chromatofocusing analysis, each α-glucosidase from preclimacteric bananas was found to be of pI > 7.4, which disappeared upon ripening, although another form with pI 5 as a major component appeared instead. It is unknown whether this phenomenon is due to protein de novo synthesis and/or post-translational modifications of the enzyme. A large amount of acid α-glucosidase from preclimacteric bananas was shown to be a glycoprotein that bound to a Con A-Sepharose column. While this type of enzyme decreased during ripening, it remained a possibility that sugar components of the enzyme might be processed during ripening. The neutral α-glucosidase had no affinity to the column through ripening. These results provide preliminary information on the mechanism of appearance of α-glucosidase multiforms as well as on a useful strategy for purification of acid and neutral α-glucosidases from banana pulp at various stages of ripening.
収録刊行物
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- Agricultural and Biological Chemistry
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Agricultural and Biological Chemistry 55 (4), 1089-1094, 1991
公益社団法人 日本農芸化学会
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詳細情報 詳細情報について
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- CRID
- 1390282681437171840
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- NII論文ID
- 110006325492
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- NII書誌ID
- AA00515312
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- COI
- 1:CAS:528:DyaK3MXkt1Kjurw%3D
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- ISSN
- 18811280
- 00021369
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- 本文言語コード
- en
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- データソース種別
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- JaLC
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- 使用不可