Makale detayı · 2008
Purification and Characterization of Peroxidase from Cauliflower Brassica oleracea L var botrytis Buds
Dergi
Protein & Peptide LettersISSN 0929-8665
ISSN kaydı başka bir dergiye işaret ediyor; ad YÖKSİS kaydından.
- Yıl
- 2008
- Tür
- article
Veri kaynağı ayrımı
- YÖKSİS YÖKSİS makale kaydı
- YÖKSİS dergi adı Protein & Peptide Letters
- Katalog eşleşmesi (ISSN) Protein and Peptide Letters
- OpenAlex OpenAlex zenginleştirmesi (özet, atıf, konular)
Özet
OpenAlex · İngilizce
Peroxidases (EC 1.11.1.7; donor: hydrogen peroxide oxidoreductase) are part of a large group of enzymes. In this study, peroxidase, a primer antioxidant enzyme, was purified with 19.3 fold and 0.2% efficiency from cauliflower (Brassica oleracea L.) by ammonium sulphate precipitation, dialysis, CM-Sephadex ion-exchange chromatography and Sephadex G-25 purification steps. The substrate specificity of peroxidase was investigated using 2,2'-azino-bis(3-ethylbenz-thiazoline-6-sulphonic acid) (ABTS), 2-methoxyphenol (guaiacol), 1,2-dihydroxybenzene (catechol), 1,2,3-trihyidroxybenzene (pyrogallol) and 4-methylcatechol. Also, optimum pH, optimum temperature, optimum ionic strength, stable pH, stable temperature, thermal inactivation conditions were determined for guaiacol/H(2)O(2), pyrogallol/H(2)O(2), ABTS/H(2)O(2), catechol/H(2)O(2) and 4-methyl catechol/H(2)O(2) substrate patterns. The molecular weight (M(w)) of this enzyme was found to be 44 kDa by gel filtration chromatography method. Native polyacrylamide gel electrophoresis (PAGE) was performed for isoenzyme determination and a single band was observed. K(m) and V(max) values were calculated from Lineweaver-Burk graph for each substrate patterns.
Konular
Atıflar
OpenAlex cited_by_count. WoS veya Scopus atıf sayısı değildir; o kaynaklar için ayrı kolon yoktur.
120 atıf
OpenAlex cited_by_count (önbellek / veritabanı)
Yerel katalogda bu makaleye atıf yapan 178 yayın (OpenAlex referans eşleşmesi; tam dünya listesi değildir).
- DPPH Radical Scavenging Assay 2023
- Metal Ions, Metal Chelators and Metal Chelating Assay as Antioxidant Method 2022
- Antioxidants: a comprehensive review 2025
- Synthesis and Carbonic Anhydrase Isoenzymes I II IX and XII Inhibitory Effects of Dimethoxybromophenol Derivatives Incorporating Cyclopropane Moieties 2015
- Synthesis and Carbonic Anhydrase Isoenzymes I II IX and XII Inhibitory Effects of Dimethoxybromophenol Derivatives Incorporating Cyclopropane Moieties 2015
- Synthesis and Carbonic Anhydrase Isoenzymes I II IX and XII Inhibitory Effects of Dimethoxybromophenol Derivatives Incorporating Cyclopropane Moieties 2015
- Synthesis and Carbonic Anhydrase Isoenzymes I, II, IX, and XII Inhibitory Effects of Dimethoxybromophenol Derivatives Incorporating Cyclopropane Moieties 2014
- The effect of caffeic acid phenethyl ester (CAPE) on metabolic enzymes including acetylcholinesterase, butyrylcholinesterase, glutathione S-transferase, lactoperoxidase, and carbonic anhydrase isoenzymes I, II, IX, and XII 2016
- The effect of caffeic acid phenethyl ester (CAPE) on metabolic enzymes including acetylcholinesterase, butyrylcholinesterase, glutathione S-transferase, lactoperoxidase, and carbonic anhydrase isoenzymes I, II, IX, and XII 2016
- The effect of caffeic acid phenethyl ester CAPE on metabolic enzymes including acetylcholinesterase butyrylcholinesterase glutathione S transferase lactoperoxidase and carbonic anhydrase isoenzymes I II IX and XII 2016