Isolation and Characterization of a Serine Proteinase, Inactivating m-Subunit of Lactate Dehydrogenase, from Penicillium citrinum KE-1
スポンサーリンク
概要
- 論文の詳細を見る
A selective inactivating enzyme for the m-subunit of lactate dehydrogenase (LDH) was found in the culture filtrate of Penicillium citrinum KE-1, newly isolated from soil. The enzyme was purified from the culture filtrate by ammonium sulfate fractionation, column chromatography on CM-Sepharose CL-6B, and gel filtration on Sephadex G-100. The purification was 124-fold with an activity yield of 81%. The purified enzyme gave a single band, corresponding to a molecular weight of 32,000, on SDS polyacrylamide gel electrophoresis, and the isoelectric point was 9.5. The enzyme specifically inactivated the m-subunit of LDH but showed no activity on the h-subunit of LDH. The enzyme, named KE-1 proteinase, proved to be a serine-type proteinase. Limited proteolysis of native m-subunit of LDH was assumed to result in a loss of enzyme activity.
- 社団法人日本農芸化学会の論文
- 1994-04-23
著者
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Okabe Hiroaki
Department of Cardiology, Juntendo University School of Medicine, and Department of Laboratory Medic
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Murao Sawao
Department Of Agricultural Chemistry College Of Agriculture University Of Osaka Prefecture
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Murao Sawao
Department Of Applied Microbial Technology Kumamoto Institute Of Technology
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Okabe H
Kumamoto Univ. Kumamoto Jpn
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Kaneda N
Kumamoto Inst. Technol. Kumamoto Jpn
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Watazu Yoshifumi
Research and Development Center, International Reagents Corporation
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Nagamatsu Katashi
Research and Development Center, International Reagents Corporation
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Shirahase Yasushi
Research and Development Center, International Reagents Corporation
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Kaneda Nobuaki
Research and Development Center, International Reagents Corporation
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Okabe Hiroaki
Department Of Cardiology Juntendo University School Of Medicine And Department Of Laboratory Medicin
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Watazu Y
International Reagents Corp. Kobe Jpn
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Shirahase Yasushi
Research And Development Center International Reagents Corporation
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