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

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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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:
sepiapterin deaminase
silkworm
Online Access:https://doi.org/10.1515/pteridines.1998.9.1.18
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spelling doaj-a2cc15deae274c2e8d5be9d85ea0dc832021-09-05T14:00:00ZengDe GruyterPteridines0933-48072195-47201998-02-0191182110.1515/pteridines.1998.9.1.18Purification and Characterization of Sepiapterin Deaminase from the Silkworm, Bombyx moriSawada Hiroshi0Kanekatsu Motoki1Nakagoshi Motoko2Dohke Kenjiro3Iino Teruhiko4Takikawa Shin-Ichiro5Biological Laboratory, Center of Liberal Arts and Sciences, Kitasato University, Kitasato 1-15-1, Sagamihara city, Kanagawa 228, JapanBiological Laboratory, Center of Liberal Arts and Sciences, Kitasato University, Kitasato 1-15-1, Sagamihara city, Kanagawa 228, JapanBiological Laboratory, Center of Liberal Arts and Sciences, Kitasato University, Kitasato 1-15-1, Sagamihara city, Kanagawa 228, JapanBiological Laboratory, Center of Liberal Arts and Sciences, Kitasato University, Kitasato 1-15-1, Sagamihara city, Kanagawa 228, JapanDepartment of General Education, Nihon University, Sakurajosui 3-25-40, Setagaya-ku, Tokyo 156, JapanBiological Laboratory, Center of Liberal Arts and Sciences, Kitasato University, Kitasato I-IS-I, Sagamihara city, Kanagawa 228, JapanSepiapterin 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 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 have an important function on the silkworm.https://doi.org/10.1515/pteridines.1998.9.1.18sepiapterin deaminasesilkworm
collection DOAJ
language English
format Article
sources DOAJ
author Sawada Hiroshi
Kanekatsu Motoki
Nakagoshi Motoko
Dohke Kenjiro
Iino Teruhiko
Takikawa Shin-Ichiro
spellingShingle Sawada Hiroshi
Kanekatsu Motoki
Nakagoshi Motoko
Dohke Kenjiro
Iino Teruhiko
Takikawa Shin-Ichiro
Purification and Characterization of Sepiapterin Deaminase from the Silkworm, Bombyx mori
Pteridines
sepiapterin deaminase
silkworm
author_facet Sawada Hiroshi
Kanekatsu Motoki
Nakagoshi Motoko
Dohke Kenjiro
Iino Teruhiko
Takikawa Shin-Ichiro
author_sort Sawada Hiroshi
title Purification and Characterization of Sepiapterin Deaminase from the Silkworm, Bombyx mori
title_short Purification and Characterization of Sepiapterin Deaminase from the Silkworm, Bombyx mori
title_full Purification and Characterization of Sepiapterin Deaminase from the Silkworm, Bombyx mori
title_fullStr Purification and Characterization of Sepiapterin Deaminase from the Silkworm, Bombyx mori
title_full_unstemmed Purification and Characterization of Sepiapterin Deaminase from the Silkworm, Bombyx mori
title_sort purification and characterization of sepiapterin deaminase from the silkworm, bombyx mori
publisher De Gruyter
series Pteridines
issn 0933-4807
2195-4720
publishDate 1998-02-01
description 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 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 have an important function on the silkworm.
topic sepiapterin deaminase
silkworm
url https://doi.org/10.1515/pteridines.1998.9.1.18
work_keys_str_mv AT sawadahiroshi purificationandcharacterizationofsepiapterindeaminasefromthesilkwormbombyxmori
AT kanekatsumotoki purificationandcharacterizationofsepiapterindeaminasefromthesilkwormbombyxmori
AT nakagoshimotoko purificationandcharacterizationofsepiapterindeaminasefromthesilkwormbombyxmori
AT dohkekenjiro purificationandcharacterizationofsepiapterindeaminasefromthesilkwormbombyxmori
AT iinoteruhiko purificationandcharacterizationofsepiapterindeaminasefromthesilkwormbombyxmori
AT takikawashinichiro purificationandcharacterizationofsepiapterindeaminasefromthesilkwormbombyxmori
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