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Purified s-GOT and m-GOT fractions showed\nremains of a small amount of impurities on disc electrophoregrams. Zymograms of s-GOT\nand m-GOT fractions on starch-gel showed their specific polarities. s-GOT fraction yielded\nfour bands on the anode side of the zymogram, whereas the m-GOT fraction yielded two\nbands on the cathode side. Purification of GOT of eel liver which was performed in order\nto compare with the GOT isozymes of tilapia liver. The GOT isozymes of eel liver had\nalmost same characteristics as that of the tilapia liver.\nKinetic studies on s-GOT and m-GOT from liver of T. zillii were performed. 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Purification of Aspartate Aminotransferase in the Liver of Tilapia zillii
http://hdl.handle.net/10232/13282
http://hdl.handle.net/10232/1328216f8d594-48b9-40fd-b1d7-d116ea03fd0d
名前 / ファイル | ライセンス | アクション |
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Item type | 紀要論文 / Departmental Bulletin Paper(1) | |||||
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公開日 | 2012-05-07 | |||||
タイトル | ||||||
タイトル | Purification of Aspartate Aminotransferase in the Liver of Tilapia zillii | |||||
別言語のタイトル | ||||||
その他のタイトル | Tilapia zillii肝臓中のアスパルテート・アミノトランスフェラーゼの精製 | |||||
著者 |
SAMESHIMA, Muneo
× SAMESHIMA, Muneo× NAKASHIMA, Hiroyasu |
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別言語の著者 | ||||||
姓名 | 鮫島, 宗雄 | |||||
別言語の著者 | ||||||
姓名 | 中島, 弘康 | |||||
言語 | ||||||
言語 | eng | |||||
資源タイプ | ||||||
資源タイプ識別子 | http://purl.org/coar/resource_type/c_6501 | |||||
資源タイプ | departmental bulletin paper | |||||
要約(Abstract) | ||||||
内容記述タイプ | Other | |||||
内容記述 | Partial purification of GOT isozymes from T. zillii were performed by mean of CM-cellulose column chromatography. Purified s-GOT and m-GOT fractions showed remains of a small amount of impurities on disc electrophoregrams. Zymograms of s-GOT and m-GOT fractions on starch-gel showed their specific polarities. s-GOT fraction yielded four bands on the anode side of the zymogram, whereas the m-GOT fraction yielded two bands on the cathode side. Purification of GOT of eel liver which was performed in order to compare with the GOT isozymes of tilapia liver. The GOT isozymes of eel liver had almost same characteristics as that of the tilapia liver. Kinetic studies on s-GOT and m-GOT from liver of T. zillii were performed. It was recognized that the reaction of GOT isozyme is a binary mechanism, namely, s-GOT had a strong affinity for 2-oxoglutarate, whereas m-GOT had a strong affinity for aspartate. |
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収録雑誌名 |
鹿児島大学水産学部紀要=Memoirs of Faculty of Fisheries Kagoshima University 巻 32, p. 97-107 |
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作成日 | ||||||
日付 | 1983-12-25 | |||||
ISSN | ||||||
収録物識別子タイプ | ISSN | |||||
ISSN | 0453087X | |||||
NII書誌ID(雑誌) | ||||||
収録物識別子タイプ | NCID | |||||
NC ID | AN00040498 | |||||
出版タイプ | ||||||
出版タイプ | VoR | |||||
出版タイプResource | http://purl.org/coar/version/c_970fb48d4fbd8a85 | |||||
NDC | ||||||
主題Scheme | NDC | |||||
主題 | 663 | |||||
公開者・出版者 | ||||||
出版者 | 鹿児島大学 | |||||
公開者よみ | ||||||
公開者よみ | カゴシマ ダイガク | |||||
公開者別名 | ||||||
公開者別名 | Kagoshima University |