WEKO3
アイテム
サバ幽門垂カルボキシペプチダーゼに関する研究
http://hdl.handle.net/10232/14340
http://hdl.handle.net/10232/143400b75fe48-dcff-438c-ba42-b3376bf71cd7
| 名前 / ファイル | ライセンス | アクション |
|---|---|---|
AN00040498_v11n2_p111-151.pdf (17.7 MB)
|
|
| Item type | 紀要論文 / Departmental Bulletin Paper(1) | |||||
|---|---|---|---|---|---|---|
| 公開日 | 2015-06-24 | |||||
| タイトル | ||||||
| タイトル | サバ幽門垂カルボキシペプチダーゼに関する研究 | |||||
| タイトル言語 | ja | |||||
| タイトル | ||||||
| タイトル | Biochemical Studies on Carboxypeptidase Contained in the Pyloric Coeca of Mackerel, Scomber Japonicus | |||||
| タイトル言語 | en | |||||
| 著者 |
大城, 善太郎
× 大城, 善太郎 |
|||||
| 言語 | ||||||
| 言語 | jpn | |||||
| 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 | |||||
| アクセス権 | ||||||
| アクセス権 | open access | |||||
| アクセス権URI | http://purl.org/coar/access_right/c_abf2 | |||||
| 要約 | ||||||
| 内容記述タイプ | Other | |||||
| 内容記述 | It was, at the outset, demonstrated that the precipitate yielded abundantly on the dialysis of a saline extract of the pyloric coeca of mackerel, Scomber japonicus, showed an enzymatic activity which catalyses both the hydrolysis of chloroacetyl-L-tyrosine and the asymmetric hydrolysis of chloroacetyl-DL-phenylalanine. The active enzymatic principle was assumed to be a carboxypeptidase (CPase). Zone electrophoresis indicated that a major constituent of the precipitate was repsonsible for the enzyme activity. The active priciple was separated through a well arranged employment of the DEAE-cellulose column chromatography, and an ultracentrifugally homogenous CPase was isolated. The chromatogram obtained through this procedure was found to be quite different from that obtained from the bovine pancreatic CPase under the same experimental conditions. |
|||||
| 内容記述言語 | en | |||||
| 要約 | ||||||
| 内容記述タイプ | Other | |||||
| 内容記述 | By the purification procedure, the specific activity of the enzyme was increased as much as 4.3 times. A sedimentation constant (st) of 3.25×10^[-13] was obtained by the ultracentrifugation. The molecular weight was calculated to be 23,500, which was definitely smaller than that of the bovine pancreatic CPase, 34,000. This fact suggests that these two forms of CPase consist of different types of proteins. Optimal pH and temperature for the hydrolysis of carbobenzoxyglycyl-L-phenylalanine were found to be 8.0 and 35-40°C respectively. Furthermore, the mackerel pyloric coeca CPase was ascertained to be a type of metal enzyme. Effects of various metals on the activity of this enzyme were examined. No effect was brought about by calcium and magnesium. The activity was inhibited by manganese and zinc as much as 50 per cent, while it was five times activated by cobalt. On the other hand, the activity was arrested by the chelating agent EDTA. The enzyme inactivated in this way was reactivated by calcium, magnesium and, particularly, by cobalt, but not by zinc. The mackerel pyloric coeca CPase differs also in this respect from the bovine pancreatic CPases, although the substrate specificities of these two enzymes are identical. |
|||||
| 内容記述言語 | en | |||||
| 要約 | ||||||
| 内容記述タイプ | Other | |||||
| 内容記述 | Judging from the way of the asymmetric hydrolysis of chloroacetyl-DL-phenylalanine, chloroacetyl-DL-tyrosine, and chloroacetyl-DL-leucine, the pyloric coeca CPases is assumed to be a type of CPase-A, although it apparently differs from the bovine pancreatic CPase-A in the nature of the enzyme protein. Finally, some physico-chemical properties were investigated on both the intact and the cobalt-treated pyloric coeca CPase. The kinetic constants, such as Michaelis constant K_m, V_max, activation energies E_A, and the various velocity constants, were determined in the case of the hydrolysis of carbobenzoxy-glycyl-L-phenylalanine, and these kinetic constants of the two types of the enzyme were studied comparatively to elucidate the mechanism of the participation of cobalt ion in the activation of the enzyme. The activation energies, k_1/k_1, and k_2/k_1 decreased by treatment of the enzyme with cobalt ion, together with the corresponding, directly proportional diminution of K_m. Judging from these facts, it is postulated that a close combination of cobalt ion with the active center or the enzyme occurs quite readily to form a favorable structure of the active site and the stable ES-complex. |
|||||
| 内容記述言語 | en | |||||
| 収録雑誌名 |
ja : 鹿児島大学水産学部紀要 en : Memoirs of Faculty of Fisheries Kagoshima University 巻 11, 号 2, p. 111-151, 発行日 1962-12-25 |
|||||
| 作成日 | ||||||
| 日付 | 1962-12-25 | |||||
| 日付タイプ | Issued | |||||
| ISSN | ||||||
| 収録物識別子タイプ | PISSN | |||||
| 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 | |||||
| 出版者言語 | ja | |||||
| 公開者・出版者 | ||||||
| 出版者 | Kagoshima University | |||||
| 出版者言語 | en | |||||
