Purification and Characterization of Sepiapterin Deaminase from the Silkworm, Bombyx mori

Sepiapterin deaminase has been purified approximately 6,000-told from the larval integument of the lemon mutant of the silkworm by several column chromatographic procedures. Sepiapterin and isosepiapterin were active substrates among various pteridines tested. The molecular mass of this enzyme was e...

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Bibliographic Details
Main Authors: Sawada Hiroshi, Kanekatsu Motoki, Nakagoshi Motoko, Dohke Kenjiro, Iino Teruhiko, Takikawa Shin-Ichiro
Format: Article
Language:English
Published: De Gruyter 1998-02-01
Series:Pteridines
Subjects:
Online Access:https://doi.org/10.1515/pteridines.1998.9.1.18