Characterization of a Phenol Oxidase from <i>Cryptococcus neoformans</i> var. <i>neoformans</i>

• Ikeda Reiko

  Department of Microbiology, Meiji College of Pharmacy

• Shinoda Takako

  Department of Microbiology, Meiji College of Pharmacy

• Morita Takashi

  Department of Biochemistry, Meiji College of Pharmacy

• Jacobson Eric S.

  Research Service, McGuire Veterans Affairs Medical Center

抄録

In Cryptococcus neoformans, enzymic oxidation of various catechols leads to melanin, a proposed virulence factor. A phenol oxidase enzyme of Cryptococcus neoformans var. neoformans produced at 25C has been purified from an ultracentrifugal supernatant of an extract of broken cells. Hydrophobic interaction chromatography followed by anion-exchange column chromatography allowed purification of the phenol oxidase. The molecular weight of the enzyme estimated by gel filtration was about 80, 000 and a dimeric species (Mw=160, 000) was suggested. The isoelectric point of the protein was approximately 4.1. An NH₂-terminal 31 amino acid sequence was determined using phenol oxidase electroblotted onto a PVDF membrane after nondenaturing gel electrophoresis. Upon searching the Peptide Institute (Osaka) data base, no proteins with high degrees of homology were found.

収録刊行物

• MICROBIOLOGY and IMMUNOLOGY

  MICROBIOLOGY and IMMUNOLOGY 37 (10), 759-764, 1993

  Center For Academic Publications Japan

詳細情報

• CRID: 1571698603035194880
• NII論文ID: 130003483927
• ISSN: 03855600
• Web Site: https://jlc.jst.go.jp/DN/JALC/00079968935?from=CiNii
• 本文言語コード: en
• データソース種別:
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