Covalent structure of turnip peroxidase 7. Tryptic peptides.
Mazza. G G; Welinder. K G KG
Key Findings
- Turnip peroxidase 7’s full 296‑residue sequence was determined through trypsin digestion and peptide analysis.
- Four disulfide bridges and the single carbohydrate attachment site were identified.
- The work was complemented by additional fragments made with cyanogen bromide and chymotrypsin.
Practical Outcomes
- There are no actionable takeaways for human health or biohacking; the research is purely a basic biochemistry study of a plant protein.
Summary
The study maps the exact amino‑acid sequence of a plant enzyme called turnip peroxidase 7 using lab techniques, but it doesn’t discuss any health‑related peptide or give advice you can use for longevity or performance.
Abstract
Turnip isoperoxidase TP 7 had its hemin group removed and was cleaved by trypsin. The digest was fractionated by gel filtration and high-voltage paper electrophoresis and yielded 24 peptides, which counted for all 296 amino acid residues of the enzyme. Sequence analyses on the tryptic peptides and, when necessary, on their thermolytic derivatives were carried out by manual Edman degradation followed by dansylation or by quantitative amino acid analysis of thiazolinones converted by HI. The four disulfide bridges and the only site of carbohydrate attachment of turnip peroxidase 7 are located. The present analysis of tryptic peptides has been complemented by cyanogen bromide fragments cleaved by chymotrypsin as described in the accompanying paper.
Study Information
pubmed
1980
10.1111/j.1432-1033.1980.tb04744.x