Studies on the Lipoprotein Lipases of Microorganisms
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- SAIKI Takashi
- Department of Agricultural Chemistry, Faculty of Agriculture, The University of Tokyo
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- TAKAGI Yoshimasa
- Department of Agricultural Chemistry, Faculty of Agriculture, The University of Tokyo Amano Pharmaceutical Co. Ltd.
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- SUZUKI Teruji
- Department of Agricultural Chemistry, Faculty of Agriculture, The University of Tokyo Amano Pharmaceutical Co. Ltd.
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- NARASAKI Teiichi
- Department of Agricultural Chemistry, Faculty of Agriculture, The University of Tokyo Department of Agricultural Chemistry, Faculty of Agriculture, Kagawa University
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- TAMURA Gakuzo
- Department of Agricultural Chemistry, Faculty of Agriculture, The University of Tokyo
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- ARIMA Kei
- Department of Agricultural Chemistry, Faculty of Agriculture, The University of Tokyo
書誌事項
- タイトル別名
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- Part IV Purification and General Properties of the Lipoprotein Lipase Produced by <i>Mucor javanicus</i>
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説明
Mucor javanicus IAM 6108 was cultivated aerobically at large scale in the medium containing corn steep liquor 3.0%, soluble starch 1.0%, soybean yuto 1.0% and inorganic salts, and the lipoprotein lipase produced was recovered by addition of ammonium sulfate (0.7 saturation). From this crude preparation, the enzyme was purified about 13times, through ammonium sulfate fractionation (0_??_0.4 saturation), precipitation at pH 4.0, ethanol precipitation (80%) and Sephadex G-200 gel filtration. The purified lipoprotein lipase was sedimented as single peak in ultracentrifugal analysis in the presence of 1.0% sodium dodecylsulfate. The enzymatic properties of the purified enzyme was as follows; optimum pH was 7.0, stable pH range was from 5.0 to 7.0, optimum temperature was 40°C, inactivated rapidly above 50°C. The lipoprotein lipase activity was inhibited by 75% and 88% by 10-2M taurocholate and 1.0M NaCl, respectively. ZnCl2, CuCl2, Pb(NO3)2, and SnCl2 at 10-3M showed complete inhibition. The ratio of lipoprotein lipase to lipase activity was 10:1. Lipoprotein lipase activity was dependent on the concentration of blood plasma which could be substituted by bovine serum albumin or egg albumin to a certain degree. The results suggesting the preferential α-fatty acid hydrolysis was obtained.
収録刊行物
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- Agricultural and Biological Chemistry
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Agricultural and Biological Chemistry 33 (3), 414-423, 1969
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
- 1390282681444190976
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- NII論文ID
- 130003415408
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- COI
- 1:CAS:528:DyaF1MXkt1Omsbg%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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- 抄録ライセンスフラグ
- 使用不可
