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 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 estimat...

Full description

Saved in:
Bibliographic Details
Published in:Pteridines 1998-02, Vol.9 (1), p.18-21
Main Authors: Sawada, Hiroshi, Kanekatsu, Motoki, Nakagoshi, Motoko, Dohke, Kenjiro, Iino, Teruhiko, Takikawa, Shin-Ichiro
Format: Article
Language:English
Subjects:
Sepiapterin deaminase
Silkworm
Citations: Items that cite this one
Online Access:Get full text
Tags: Add Tag
No Tags, Be the first to tag this record!
Description
Summary:Sepiapterin deaminase has been purified approximately 6,000-told from the larval integument of the 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 estimated to be 74 kDa by SDS-PAGE and 70 kDa by gel filtration, suggesting that the native form of the enzyme is monomeric protein . All silkworm strains, to the best of our knowledge, had an activity of the enzyme and the enzyme was widely distributed in the larval tissues. Sepiapterin deaminase may an important function on the silkworm.
ISSN:0933-4807
2195-4720
DOI:10.1515/pteridines.1998.9.1.18