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Hayakawa T, Kanematsu S, Asada K. Purification and characterization of thylakoid-bound Mn-superoxide dismutase in spinach chloroplasts. Planta. 1985;166(1):111-6doi: 10.1007/BF00397393.
Hayakawa, T., Kanematsu, S., & Asada, K. (1985). Purification and characterization of thylakoid-bound Mn-superoxide dismutase in spinach chloroplasts. Planta, 166(1), 111-6. https://doi.org/10.1007/BF00397393
Hayakawa, T, et al. "Purification and characterization of thylakoid-bound Mn-superoxide dismutase in spinach chloroplasts." Planta vol. 166,1 (1985): 111-6. doi: https://doi.org/10.1007/BF00397393
Hayakawa T, Kanematsu S, Asada K. Purification and characterization of thylakoid-bound Mn-superoxide dismutase in spinach chloroplasts. Planta. 1985 Sep;166(1):111-6. doi: 10.1007/BF00397393. PMID: 24241319.
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Planta. 1985 Sep;166(1):111-6. doi: 10.1007/BF00397393.

Purification and characterization of thylakoid-bound Mn-superoxide dismutase in spinach chloroplasts.

Planta

T Hayakawa, S Kanematsu, K Asada

Affiliations

  1. Research Institute for Food Science, Kyoto University, 611, Uji, Kyoto, Japan.

PMID: 24241319 DOI: 10.1007/BF00397393

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.

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