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Purification and N-terminal amino acid sequence of solanapyrone synthase, a natural Diels-Alderase from Alternaria solani.

作者信息

Katayama Kinya, Kobayashi Tomonori, Chijimatsu Masao, Ichihara Akitami, Oikawa Hideaki

机构信息

School of Veterinary Medicine, Faculty of Veterinary Science, Nippon Veterinary and Life Science University, Musashino-shi, Tokyo 180-8602, Japan.

出版信息

Biosci Biotechnol Biochem. 2008 Feb;72(2):604-7. doi: 10.1271/bbb.70600. Epub 2008 Feb 7.

DOI:10.1271/bbb.70600
PMID:18256508
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.

摘要

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