書誌事項
- タイトル別名
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- Catalase from Black Matpe Sprouts: Further Characterization of the Enzyme
- コクリョクトウ モヤシカタラーゼ コウソガクテキ タンパク シツテキ セイシツ
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The enzymatic and protein-chemical properties were investigated in catalase purified from black matpe (Phaseolus mungo L. var. radiatus Bak) sprouts. The catalase had a broad optimum pH of 7 to 9 in 0.05M phosphate buffer and Tris-HCl buffer. The enzyme was very labile below pH 6.0 but relatively stable at pH 9.0. It was slowly inactivated by dilution and was rapidly inactivated by 8M urea. About 20% of the enzyme activity was lost by freezing and thawing. Low molecular weight nitrogen compounds including NH2OH•HCl, NaN3, KCN, NaNO2, CS(NH2)2 and 3-amino-1, 2, 4-triazole were potent inhibitors of the enzyme. The sedimentation coefficient (s20, W) of the enzyme was 12.1 s. The molecular weight was determined as 187, 000 by the sedimentation equilibrium method using a partial specific volume of 0.72. The protein was characterized by a high content of serine, glutamic acid and glycine, as well as by a low content of cystine and methionine.
収録刊行物
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- 日本農芸化学会誌
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日本農芸化学会誌 58 (4), 381-383, 1984
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
- 1390001204507217152
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- NII論文ID
- 130001229820
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- NII書誌ID
- AN00196191
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- ISSN
- 18836844
- 00021407
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- NDL書誌ID
- 2986656
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- 本文言語コード
- ja
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- データソース種別
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- JaLC
- NDL
- Crossref
- CiNii Articles
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- 抄録ライセンスフラグ
- 使用不可