Crystallization and Properties of _L-Phenylalanine Ammonia-lyase from Rhodosporidium toruloides(Microbiology & Fermentation Industry)
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概要
- 論文の詳細を見る
_L-Phenylalanine ammonia-lyase was crystallized for the first time from a cell-free extract of Rhodosporidium toruloides IFO 0559. Heat treatment at 50℃ for 5 min was a smart step for enzyme purification. Column chromatographies with DEAE-cellulose and hydroxyapatite, and gel filtration on a Sephadex G-200 column were used in the subsequent purification. The enzyme was purified to a homogeneous state and crystallized as fine needles with ammonium sulfate. The crystalline enzyme was pure by both analytical ultracentrifugation and polyacrylamide gel electrophoresis. The enzyme had a 8.2 s sedimentation velocity. The molecular weight of the enzyme was 165,000 by the dual methods of sedimentation equilibrium and gel filtration. The enzyme was composed of two identical subunits with a molecular weight of 80,000.
- 社団法人日本農芸化学会の論文
- 1990-11-23
著者
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Adachi Osao
Derartment Of Blological Chemistry Faculty Of Agriculture Yamaguchi University
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Adachi Osao
Laboratory Of Applied Microbiology Department Of Biological Chemistry Faculty Of Agriculture Yamaguc
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SHINAGAWA Emiko
Laboratory of Applied Microbiology, Department of Agricultural Chemistry, Faculty of Agriculture, Ya
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Ameyama M
Department Of Biological Chemistry Faculty Of Agriculture Yamaguchi University
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Ameyama Minoru
Laboratory Of Applied Microbiology Department Of Agricultural Chemistry Faculty Of Agriculture Yamag
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Shinagawa Emiko
Department Of Chemical And Biological Engineering Ube National College Of Technology
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Matsushita Kazunobu
Laboratory Of Applied Microbiology Department Of Biological Chemistry Faculty Of Agriculture Yamaguc
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