Preparation of human manganese superoxide dismutase by tri-phase partitioning and preliminary crystallographic data

• Published in: Journal of molecular biology Vol. 219; no. 1; p. 103
• Main Authors: Deutsch, H F, Hoshi, S, Matsuda, Y, Suzuki, K, Kawano, K, Kitagawa, Y, Katsube, Y, Taniguchi, N
• Format: Journal Article
• Language: English
• Published: England 05-05-1991
• Subjects: Ammonium Sulfate; Crystallization; Humans; Isoenzymes - chemistry; Isoenzymes - isolation & purification; Isoenzymes - metabolism; Liver - enzymology; Protein Conformation; Superoxide Dismutase - chemistry; Superoxide Dismutase - isolation & purification; Superoxide Dismutase - metabolism; X-Ray Diffraction - methods
• ISSN: 0022-2836
• DOI: 10.1016/0022-2836(91)90860-9

Human liver manganese superoxide dismutase has been purified by a short procedure that includes a tri-phase partitioning step to provide materials that can be crystallized from ammonium sulfate. X-ray diffraction studies at 3 A resolution show that the crystals belong to the hexagonal space group P6(1)22 or P6(5)22, with cell dimensions a = b = 81.1 A, c = 242.2 A. Manganese superoxide dismutase levels as determined by enzymatic assay as well as by enzyme-linked immunosorbent assay indicated that considerable variations occur in different livers but the total superoxide dismutase activity (Mn superoxide dismutase plus Cu,Zn superoxide dismutase) seems to be kept at constant values.