Ascorbate Peroxidase in Tea Leaves: Occurrence of Two Isozymes and the Differences in Their Enzymatic and Molecular Properties
Clicks: 2
ID: 306772
1989
Article Quality & Performance Metrics
Overall Quality
Not rated
Combines reader engagement with the AI quality analysis. This
article has not been analysed, so there is no overall score —
reader engagement is measured and shown alongside.
Reader Engagement
Emerging Content
0.3
/100
2 views
1 readers
AI Quality Assessment
Not analyzed
Readership in this journal
EmergingRanked #65 of 94 articles by views in plant and cell physiology
Most read
Least read
Bar heights use a square-root scale.
Mint this article as an NFT
Not yet mintedCreate a permanent, verifiable on-chain record of this article on the Scimatic Network. The NFT is held in your Journament account, and you can withdraw it to your own wallet at any time.
5
SUSD
one-off · no wallet required
Abstract
Two isozymes of ascorbate (AsA) peroxidase were found in tea leaves, and one of them (AsA peroxidase II) was purified to homogeneity, as judged by polyacrylamide gel electrophoresis. AsA peroxidase II is a monomer with a molecular weight of 34,000 and contains protoheme, but it is not a glycoprotein. The enzyme showed a Soret peak at 409 run and at 420 nm when oxidized and reduced, respectively, with an a-band at 556 nm. The oxidized enzyme showed two small peaks at 478 nm and 530 nm. The peak at 478 nm disappeared when the enzyme was inactivated by depletion of AsA or by the addition of cyanide. Antibody raised against AsA peroxidase II from tea did not cross-react with guaiacol peroxidase from spinach, and antibody against the guaiacol peroxidase did not with AsA peroxidases from tea leaf. The amino acid composition and amino acid sequence of the amino-terminal region of AsA peroxidase II were determined. Little homology in terms of amino acid sequence was found between AsA peroxidase II and various guaiacol peroxidases. The enzymatic and molecular properties of the two isozymes showed distinct differences with respect to molecular weight, sensitivity to AsA-depletion, specificity for the electron donor, and other enzymatic properties.
| Reference Key |
openalex_W1833917958
Use this key to autocite in the manuscript while using
SciMatic Manuscript Manager or Thesis Manager
|
|---|---|
| Authors | Gongxiang Chen, Kozi Asada |
| Journal | plant and cell physiology |
| Year | 1989 |
| DOI |
10.1093/oxfordjournals.pcp.a077844
|
| URL | |
| Keywords | Keywords not found |
Citations
No citations found. To add a citation, contact the admin at info@scimatic.org
Comments
No comments yet. Be the first to comment on this article.