Partial purification of a thylakoid-bound enzyme using temperature-induced phase partitioning

✍ Scribed by Alvaro Sánchez-Ferrer; Roque Bru; Francisco García-Carmona

• Book ID: 102630511
• Publisher: Elsevier Science
• Year: 1990
• Tongue: English
• Weight: 444 KB
• Volume: 184
• Category: Article
• ISSN: 0003-2697
• DOI: 10.1016/0003-2697(90)90681-x

✦ Synopsis

Triton X-114 was used to partially purify broad bean polyphenol oxidase, a thylakoid membrane-bound enzyme, in latent form, free of phenolic compounds and chlorophylls, with a high recovery rate. The activation of the latent enzyme by detergents or trypsin was 10 times higher than that obtained when the enzyme was purified by other methods used in plant biochemistry, such as acetone powders and ammonium sulfate fractionation. The kinetic parameters of the latent and activated enzyme are also given.