Sterol ester hydrolytic activity of lipoprotein lipase from Pseudomonas fluoresence
書誌事項
- タイトル別名
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- Sterol ester hydrolytic activity of lipoprotein lipase from Pseudomonas fluorescence.
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The activity of sterol ester hydrolase was found in the crude enzyme preparation of lipoprotein lipase from Pseudomonas fluorescence. The enzyme was purified by ammonium sulfate fractionation and chromatographies on diethylaminoethyl (DEAE)-cellulose, Sephadex G-75 and carboxymethyl (CM)-cellulose. The lipolytic activity and sterol ester hydrolytic activity at various stages in the purification were found in the same fraction and the ratio of both activities was constant. The purified enzyme was found to be homogeneous by disc electrophoresis and SDS-polyacrylamide gel electrophoresis. Furthermore, one single protein peak which contained lipolytic and sterol ester hydrolytic activities was observed by isoelectric focusing. Therefore, it was concluded that the actions of lipoprotein lipase and sterol ester hydrolase will belong to a same enzyme protein. The action of the purified enzyme for the cholesterol esters in human plasma was investigated. Cholesterol ester was hydrolyzed completely and the rate of hydrolysis of esters of long chain fatty acids was more rapid than that of short.
収録刊行物
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- CHEMICAL & PHARMACEUTICAL BULLETIN
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CHEMICAL & PHARMACEUTICAL BULLETIN 24 (6), 1202-1208, 1976
公益社団法人 日本薬学会
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詳細情報 詳細情報について
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- CRID
- 1390282679145085952
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- NII論文ID
- 110003635119
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- NII書誌ID
- AA00602100
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- COI
- 1:CAS:528:DyaE28XkslCitb4%3D
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- ISSN
- 13475223
- 00092363
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- PubMed
- 828527
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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
- Crossref
- PubMed
- CiNii Articles
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- 抄録ライセンスフラグ
- 使用不可