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- 小野 和夫
- 山陽学園短期大学食物栄養学科
書誌事項
- タイトル別名
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- Properties of the Decarboxylase Component of Xenopus laevis Branched-chain a -Keto Acid Dehydrogenase Complex
- Properties of the decarboxylase component of Xenopus laevis branched-chain α-keto acid dehydrogenase complex
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Branched-chain a-keto acid dehydrogenase complex(BCKADC)contains decarboxylase(EL), dihydrolipoyl transacylase, and dihydrolipoyl dehydrogenase as catalytic components. To characterize BCKADC of amphibian, mitochondrial extract of Xenopus laevis liver was subjected to immunoblotting analysis using rat anti EL antibodies. As a result, three immunoreactive proteins were detected; the molecular mass of proteins was estimated to be 36,37 and 46 kDa. Incubation of liver mitochondria from Xenopus laevis prior to solubilization of EL resulted in no significant change in their appearance and amount. These proteins were also detected in heart of Xenopus laevis as well as liver of the amphibian. Sucrose density gradient centrifugation under the condition, which brings dissociation of BCKADC to each component enzyme, revealed that the three proteins of Xenopus laevis moved together through the gradient. The density that three proteins settled corresponded well with that of rat EL did. Present results obtained here showed that EL of Xenopus laevis contains three proteins at least, and the 47 kDa protein corresponds to EL a subunit in comparison with molecular mass of EL a of other species.
収録刊行物
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- 山陽学園短期大学紀要
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山陽学園短期大学紀要 40 (0), 1-8, 2009
学校法人山陽学園 山陽学園短期大学
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詳細情報 詳細情報について
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- CRID
- 1390564238048770304
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- NII論文ID
- 110007610938
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- NII書誌ID
- AN10473083
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- ISSN
- 2433457X
- 13410644
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- NDL書誌ID
- 10673123
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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
- NDL
- CiNii Articles
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- 抄録ライセンスフラグ
- 使用不可