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Plant and Cell Physiology, 1987, Vol. 28, No. 6 1071-1079
© 1987

Article

Purification of Isomeric Forms of Acyl-[Acyl-Carrier-Protein]:Glycerol-3-Phosphate Acyltransferase from Greening Squash Cotyledons

Ikuo Nishida, Margrit Frentzen1, Osamu Ishizaki and Norio Murata2

National Institute for Basic Biology Myodaiji, Okazaki 444, Japan

2To whom correspondence should be addressed.

Acyl-[acyl-carrier-protein]:glycerol-3-phosphate acyltransferase was purified from greening cotyledons of squash (Cucurbita moschata Duch. cv. Shirakikuza) by [acyl-carrier proteinj-affinity column chromatography in addition to conventional purification procedures. Three isomeric forms designated as ATI, AT2 and AT3 were found: ATI was separated from the other two isomeric forms by anion-exchange column chromatography, whereas AT2 and AT3 were separated by hydroxyapatite column chromatography. ATI was purified 24,000-fold on the basis of specific activity; AT2 and AT3 were purified to single components after 40,000- and 32,000-fold purification, respectively. The isoelectric points of ATI, AT2 and AT3 at 4°C were 6.6, 5.6 and 5.5, respectively. Gel-filtration column chromatography and sodium dodecylsulfate gel electrophoresis indicated that the respective isomeric forms were monomers with apparent molecular masses of about 30 kDa, 40 kDa and 40 kDa. The isoelectric focusing of the chloroplast stroma proteins from the squash cotyledons suggested that ATI, AT2 and AT3 are all localized in the chloroplast stroma.

1 On leave from Institut für Allgemeine Botanik, Universität Hamburg, Ohnhorststraße 18, 2000 Hamburg, F.R.G.

(Received April 17, 1987; Accepted June 12, 1987)
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