Related Experiment Video
Updated: May 5, 2026

Purification of Active Photosystem I-Light Harvesting Complex I from Plant Tissues
Published on: February 3, 2023
Purification and characterization of thylakoid-bound Mn-superoxide dismutase in spinach chloroplasts
T Hayakawa1, S Kanematsu, K Asada
1Research Institute for Food Science, Kyoto University, 611, Uji, Kyoto, Japan.
Abstract:
Thylakoid-bound superoxide dismutase (SOD; EC 1.15.1.1) was solubilized by Triton X-100 from spinach and purified to a homogeneous state. The molecular weight of thylakoid-bound SOD was 52000; the enzyme was composed of two equal subunits. Its activity was not sensitive to cyanide and hydrogen peroxide, and the isolated SOD contained Mn, but neither Fe nor Cu. Thus, the thylakoid-bound SOD is a Mn-containing enzyme. The subunit molecular weight of thylakoid Mn-SOD is the highest among Mn-SODs isolated so far, a fact which might reflect its binding to the membranes.
More Related Videos
08:40Separation of Spinach Thylakoid Protein Complexes by Native Green Gel Electrophoresis and Band Characterization using Time-Correlated Single Photon Counting
Published on: February 14, 2019
11:55In Vitro Reconstitution of Light-harvesting Complexes of Plants and Green Algae
Published on: October 10, 2014