Preliminary crystallographic study of peanut peroxidase.
The cationic isozyme of peroxidase isolated from suspension cultures of peanut cells is a heme-containing and calcium-dependent glycoprotein having four covalently attached oligosaccharide chains. Attempts were made to crystallize the glycoprotein for X-ray diffraction analysis, and these have met with some success. Crystals have now been grown that are suitable for a full three-dimensional structural analysis. The crystals are thin plates and we have shown them to be of the orthorhombic space group P2(1)2(1)2(1) with a = 48.1, b = 97.2, c = 146.2 A. The crystals diffract to beyond 2.8 A resolution, appear to be stable to lengthy X-ray exposure, and contain two molecules of 40,000 daltons each in the asymmetric unit.
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Department of Biochemistry, University of California, Riverside 92521.
van Huystee
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Day
J
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Greenwood
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Larson
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Esnault
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R
McPherson
A
A
D010367:Arachis / Q000201:enzymology*; D003460:Crystallization; D007527:Isoenzymes / Q000737:chemistry*; D010544:Peroxidases / Q000737:chemistry*; D014961:X-Ray Diffraction
D007527:Isoenzymes; D010544:Peroxidases