An Arylamidase from Flavobacterium meningosepticum
スポンサーリンク
概要
- 論文の詳細を見る
An arylamidase was purified from Flavobacterium meningosepticum by a series of chromatographies on CM-cellulose, DEAE-Sephadex A-50 and Sephadex G-150. The purified enzyme appeared homogeneous on SDS-gel electrophoresis. The molecular weight of the enzyme was estimated to be more than 500, 000 dalton by using a column of Sepharose 4B and to be 62, 000 when checked by SDS-gel electrophoresis. The enzyme was most active at pH 7.5 toward Leu-β-naphthylamide (Leu-β-NA). It catalyzed the hydrolysis of not only various amino acid-β- naphthylamides but also some peptides, but the hydrolysis rate of the latter substrates was quite low. Cys-di-β-naphthylamide was split by this enzyme at an optimal pH of 6.2. Incubation of oxytocin with the enzyme resulted in a decrease in the biological activity, indicating that this arylamidase possesses an oxytocinase (cystyl aminopeptidase)-like activity.
- 社団法人 日本農芸化学会の論文
著者
-
YOSHIMOTO Tadashi
Faculty of Pharmaceutical Sciences, Nagasaki University
-
TSURU Daisuke
Faculty of Pharmaceutical Sciences, Nagasaki University
-
Yoshimoto Tadashi
Faculty Of Pharmaceutical Sciences Nagasaki University
-
Tsuru Daisuke
Faculty Of Pharmaceutical Sciences Nagasaki University
関連論文
- Proline-specific Endopeptidase from Flavobacterium meningosepticum: Physicochemical Properties
- Purification and Some Properties of a Bacteriolytic Enzyme Produced by Bacillus sp. ML-208
- Affinity chromatographic purification of human lysozyme,with special reference to human leukemia lysozyme
- Partial Purification and Characterization of Two β-Glucuronidases from Alcaligenes NG-11(Biological Chemistry)
- Purification and Comparison of Two Types of β-Galactosidases from Aspergillus oryzae
- Formaldehyde Dehydrogenase from Pseudomonas putida: The Role of A Cysteinyl Residue in the Enzyme Activity(Biological Chemistry)
- FORMALDEHYDE DEHYDROGENASE FROM PSEUDOMONAS PUTIDA : CHARACTERIZATION AS A ZINC METALLOENZYME AND THE REACTION MECHANISM
- PYROGLUTAMYL PEPTIDASE FROM CHICKEN LIVER : PURIFICATION AND SOME PROPERTIES
- AN INHIBITOR FOR POST-PROLINE CLEAVING ENZYME ; DISTRIBUTION AND PARTIAL PURIFICATION FROM PORCINE PANCREAS
- PROLINE SPECIFIC PEPTIDASES OF MICROBIAL ORIGIN
- Substrate Specificity of Formaldehyde Dehydrogenase from Pseudomonas putida
- An Arylamidase from Flavobacterium meningosepticum
- Convenient Method for Estimation of Kinetic Parameters from Time Course Analysis of EnzymeReactions with a Microcomputer