書誌事項
- タイトル別名
-
- Electrophoretic properties of mitochondrial monoamine oxidase in monkey liver.
- デンキ エイドウホウ ニ ヨル サル カンゾウ ミトコンドリア ニ フクマレル
この論文をさがす
抄録
Monkey liver monoamine oxidase (MAO) was predominantly the B-form enzyme from the observed differences in substrate specificities and differences in sensitivities to MAO inhibitors. It is known that a MAO inhibitor, pargyline, binds to MAO irreversibly in the molar ratio of 1: 1. 3H-pargyline was used as a marker to determine the existance of MAO. The molecular weight of MAO in monkey liver mitochondria was investigated by SDS-polyacrylamide gel electrophoresis after solubilization of 3H-pargyline binding mitochondria with 6% sodium dodecyl sulphate (SDS). The subunit molecular weight was found to be 60, 000. The molecular weight determined from the electrophoretic mobility on several concentrations of gels by disc gel electrophoresis in the absence of SDS was found to be 120, 000. These results indicate that monkey liver mitochondrial MAO exists as a dimer. Isoelectric focusing of the enzyme after solubilization with 0.1% Triton X-100 and 0.75% Triton X-100 and 0.75% Lubrol showed that it had a pI value near 6.5. Similar pI values were obtained for enzyme preparations solubilized with 0.75% Triton X-100 after treatment with phospholipase A or methylethylketone. These results suggest that the pI value of MAO in monkey liver mitochondria does not depend on the properties of detergents used to solubilize the enzyme preparation.
収録刊行物
-
- 日本薬理学雑誌
-
日本薬理学雑誌 90 (1), 23-31, 1987
公益社団法人 日本薬理学会
- Tweet
キーワード
詳細情報 詳細情報について
-
- CRID
- 1390001204273711104
-
- NII論文ID
- 130000759450
-
- NII書誌ID
- AN00198335
-
- ISSN
- 13478397
- 00155691
-
- NDL書誌ID
- 3137346
-
- PubMed
- 3653801
-
- 本文言語コード
- ja
-
- データソース種別
-
- JaLC
- NDL
- Crossref
- PubMed
- CiNii Articles
-
- 抄録ライセンスフラグ
- 使用不可