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Purification and N-terminal amino acid sequence of solanapyrone synthase, a natural diels-alderase from Alternaria solani

Bioscience, Biotechnology and Biochemistry (2008) 72(2) 604-607
DOI: 10.1271/bbb.70600
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Abstract

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.

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CITATION STYLE

APA

Katayama, K., Kobayashi, T., Chijimatsu, M., Ichihara, A., & Oikawa, H. (2008). Purification and N-terminal amino acid sequence of solanapyrone synthase, a natural diels-alderase from Alternaria solani. Bioscience, Biotechnology and Biochemistry, 72(2), 604–607. https://doi.org/10.1271/bbb.70600

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