Proteolytic conversion of xanthine dehydrogenase from the NAD-dependent type to the O2-dependent type. Amino acid sequence of rat liver xanthine dehydrogenase and identification of the cleavage sites of the enzyme protein during irreversible conversion by trypsin.-Reference-Cited by-同舟云学术

Proteolytic conversion of xanthine dehydrogenase from the NAD-dependent type to the O2-dependent type. Amino acid sequence of rat liver xanthine dehydrogenase and identification of the cleavage sites of the enzyme protein during irreversible conversion by trypsin.

Published:1990-08 Issue:24 Volume:265 Page:14170-14175
ISSN:0021-9258
Container-title:Journal of Biological Chemistry
language:en
Short-container-title:Journal of Biological Chemistry

Author:

Amaya Y.,Yamazaki K.,Sato M.,Noda K.,Nishino T.,Nishino T.

Publisher

Elsevier BV

Subject

Cell Biology,Molecular Biology,Biochemistry

Reference42 articles.

1. Milk xanthine oxidase type D (dehydrogenase) and type O (oxidase). Purification, interconversion and some properties

2. Transcription termination and 3′ processing: the end is in site!

3. Flavins and Flavoproteins;Bray,1982

4. General magnetic dipolar interaction of spin-spin coupled molecular dimers. Application to an EPR spectrum of xanthine oxidase

5. Regulation of xanthine oxidase in rat liver: modifications of the enzyme activity of rat liver supernatant on storage at 20 degrees

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