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...
Main Authors: | , , , , , |
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Format: | Article |
Language: | English |
Published: |
De Gruyter
1998-02-01
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Series: | Pteridines |
Subjects: | |
Online Access: | https://doi.org/10.1515/pteridines.1998.9.1.18 |