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

Analytical Biochemistry
A Sánchez-FerrerF Garcia-Carmona

Abstract

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.

Citations

May 1, 1993·Enzyme and Microbial Technology· Galaev IYu, B Mattiasson
Feb 22, 1995·Biochimica Et Biophysica Acta·A Sánchez-FerrerF García-Carmona
May 17, 1996·Journal of Chromatography. B, Biomedical Applications·E Núñez-DelicadoF García-Carmona
Dec 5, 1998·Biochimica Et Biophysica Acta·M JiménezF García-Carmona
Feb 1, 1992·Plant Physiology·E Valero, F García-Carmona
Jun 5, 2014·Biochemistry Research International·Kamal Uddin ZaidiIshrat Naaz
Sep 6, 2011·Plant Science : an International Journal of Experimental Plant Biology·Hee-Ock BooSang-Uk Chon
Aug 7, 1998·Protein Expression and Purification·M Dahl Andersen, B L Møller
Jan 1, 1994·Critical Reviews in Biochemistry and Molecular Biology·A Sánchez-FerrerF García-Carmona
Aug 15, 1991·Analytical Biochemistry·H WalterD E Brooks
May 2, 2003·Journal of Agricultural and Food Chemistry·Sung-Yum SeoNiti Sharma
Jul 17, 2001·Journal of Agricultural and Food Chemistry·R Debowska, A Podstolski
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