AVOCADO POLYPHENOLOXIDASE: PURIFICATION, AND FRACTIONATION ON SEPHADEX THIN LAYERS
- 1 May 1970
- journal article
- Published by Wiley in Journal of Food Science
- Vol. 35 (3) , 282-285
- https://doi.org/10.1111/j.1365-2621.1970.tb12163.x
Abstract
SUMMARY: Polyphenoloxidase (PPO) was purified 28‐fold by ammonium sulfate precipitation, dialysis and gel filtration. Enzyme constants were determined with a variety of substrates. Thinlayer gel filtration resolved the crude PPO in to 5 fractions with molecular weights estima ted at 14‐, 28‐, 56‐, 112‐ and over 400‐thousand by comparison with standard proteins. Subsequent electrophoresis at 90° to the direction of gel filtration resolved the 28 × 103 MW fraction into 4 to 6 components. One of these was by. far the most active of all the isoenzymes toward all the substrate sprays tested. It is probably the activity of this isoenzyme which is reflected in kinetic data, even those obtained with relatively crude avocado PPO preparations.This publication has 9 references indexed in Scilit:
- Multiple Forms of PhenoloxidaseJournal of Food Science, 1967
- On the Purification and Properties of Mushroom Tyrosinase*The Journal of Biochemistry, 1966
- Separation of a Polyphenol Oxidase for Anthocyanin‐Degradation in EggplantJournal of Food Science, 1966
- Some Characteristics of Eggplant and Avocado PolyphenolasesJournal of Food Science, 1965
- On the heterogeneity of the tyrosinase of broad bean (Vicia faba L.)Phytochemistry, 1965
- Estimation of the molecular weights of proteins by Sephadex gel-filtrationBiochemical Journal, 1964
- Separation of Proteins by Thin-Layer Gel Filtration.Acta Chemica Scandinavica, 1964
- PROTEIN MEASUREMENT WITH THE FOLIN PHENOL REAGENTJournal of Biological Chemistry, 1951
- CONTRIBUTION TO THE KNOWLEDGE OF PLANT PHENOLASESPlant Physiology, 1937