Purification and N-Terminal Amino Acid Sequence of Solanapyrone Synthase, A Natural Diels-Alderase from Alternaria solani
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概要
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The first natural Diels-Alderase, solanapyrone synthase, was purified 1,630-fold from a crude extract. The 41-kDa protein on SDS-polyacrylamide gel electrophoresis was identified as truncated solanapyrone synthase, and its N-terminal amino acid sequence was found to be QETQNLNNFLESNAINP.
- 社団法人 日本農芸化学会の論文
著者
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KOBAYASHI Tomonori
Department of Neurosurgery, Tokyo Women's Medical University
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CHIJIMATSU MASAO
RIKEN (The Institute of Physical and Chemical Research)
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OIKAWA Hideaki
Division of Chemistry, Graduate School of Science, Hokkaido University
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ICHIHARA Akitami
Department of Bioscience and Chemistry, Faculty of Agriculture, Hokkaido University
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KATAYAMA Kinya
School of Veterinary Medicine, Faculty of Veterinary Science, Nippon Veterinary and Life Science Uni
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Katayama Kinya
School Of Veterinary Medicine Faculty Of Veterinary Science Nippon Veterinary And Life Science Unive
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