한국생물물리학회:학술대회논문집 (Proceedings of the Korean Biophysical Society Conference)

한국생물물리학회 (The Korean Biophysical Society)
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PYRANOSE OXIDASE HAVING A COVALENTLY BOUND FAD AS A COENZYME

  • Kwon, Jae-Youl (Laboratory of Biophysics, Department of Microbiology, College of Natural Sciences, and Research Center for Molecular Microbiology, Seoul National University) ;
  • Kang, Sa-Ouk (Laboratory of Biophysics, Department of Microbiology, College of Natural Sciences, and Research Center for Molecular Microbiology, Seoul National University)
  • 발행 : 1996.07.01
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초록

Flavin-peptides were purified from pyranose oxidase (EC 1.1.3.10) after tryptic- chymotryptic and tryptic digestion. The spectral and chromatographic properties of these flavin peptides showed that the FAD of pyranose oxidase appears to be bound, by way of the 8${\alpha}$-methylene group, to the N-l position of the imidazole ring of the histidine. Automated sequence analysis showed that the amino acid sequence of the tryptic-chymotryptic flavin-peptide from pyranose oxidase is Ser-Thr-X-Trp and that of the tryptic flavin-peptide is Met-Ser-Thr-X-Trp. (omitted)

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