A Novel Metalloproteinase, Almelysin, from a Marine Bacterium, Alteromonas sp. No. 3696 : Purification and Characterization
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概要
- 論文の詳細を見る
We have discovered a novel metalloproteinase, which has high activity at low temperatures, from the culture supernatant of a marine bacterium. The strain was identified as Alteromonas sp. No. 3696. The metalloproteinase, named almelysin, was purified to homogeneity from the cultured supernatant at 10℃ by two column chromatographies. About 20mg of purified almelysin was obtained from 18.4 liters of the culture supernatant. The molecular mass of almelysin was estimated to be 28 kDa by SDS-PAGE and the isoelectric point was 4.3. The optimum pH for activity of almelysin was pH 8.5-9.0 and 6.5 using casein and (7-methoxycoumarin-4-yl)acetyl(MOCAc)-Pro-Leu-Gly-Leu-(N^3-[2, 4-dinitrophenyl]-L-2, 3-diaminopropionyl)[A_2pr(Dnp)]-Ala-Arg-NH_2 as substrates, respectively. Almelysin was stable between pH 7.5-8.0 and below 40℃. The optimum temperature for the activity was observed to be 40℃ using both casein and MOCAc-Pro-Leu-Gly-Leu-A_2pr(Dnp)-Ala-Arg-NH_2 as substrates. The activity of almelysin was inhibited by such metallo chelators as EDTA and o-phenanthroline, while talopeptin, phosphoramidon, and SMPI, typical metalloproteinase inhibitors, had no effect. Almelysin primarily cleaved the Ala^<14>-Leu^<15> bond and Phe^<24>-Phe^<25> bond, and secondarily the Tyr^<16>-Leu^<17> bond in oxidized insulin B-chain. However, almelysin could not cleave the His^5-Leu^6, His^<10>-Leu^<11>, and Gly^<23>-Phe^<24> bonds, which were cleaved by other metalloproteinases. These results indicate that the substrate specificity of almelysin is different from other metalloproteinases. Interestingly, Alteromonas sp. No. 3696 strain produced another proteinase as well as almelysin at 25℃.
- 社団法人日本農芸化学会の論文
- 1997-04-23
著者
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ODA Kohei
Department of Applied Biology, Kyoto Institute of Technology
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SHIBATA Masahiro
Department of Cell Biology and Neuroscience, Osaka University Graduate School of Medicine
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Sato R
Graduate School Of Bio-application And Systems Engineering Tokyo University Of Agriculture And Techn
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Sato R
Univ. Tokyo Tokyo Jpn
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Shibata Masahiro
Department Of Biomedical Engineering University Of Tokyo
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Takahashi S
Akita Res. Inst. Food And Brewing Akita
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TAKAHASHI Saori
Department of Bioengineering, Akita Research Institute of Food and Brewing (ARIF)
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Sato Ryoichi
Central Research Institute, Maruha, Tsukuba
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Oda Kohei
Department Of Agricultural Chemistry College Of Agriculture University Of Osaka Prefecture
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Oda K
Department Of Applied Biology Faculty Of Textile Science Kyoto Institute Of Technology
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Shimada M
Univ. Electro‐communications Tokyo
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Suzuki Takahito
Biological Laboratory Faculty Of Science Nara Women's University
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Sato Ryoichi
Central Research Institute Maruha Co.
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Takahashi Saori
Department Of Applied Biology Faculty Of Textile Science Kyoto Institute Of Technology
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Shibata Masahiro
Department Of Applied Biology Faculty Of Textile Science Kyoto Institute Of Technology
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Sato Ryoichi
Central Research Institute Maruha
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