Purification of Isomeric Forms of Acyl-[Acyl-Carrier-Protein] : Glycerol-3-Phosphate Acyltransferase from Greening Squash Cotyledons
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概要
- 論文の詳細を見る
Acyl-[acyl-carrier-protein] : glycerol-3-phosphate acyltransferase was purified from greening cotyledons of squash (Cucurbita moschata Duch. cv. Shirakikuza) by [acyl-carrier protein]-affinity column chromatography in addition to conventional purification procedures. Three isomeric forms designated as AT1, AT2 and AT3 were found: AT1 was separated from the other two isomeric forms by anion-exchange column chromatography, whereas AT2 and AT3 were separated by hydroxyapatite column chromatography. AT1 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 AT1, AT2 and AT3 at 4℃ 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 AT1. AT2 and AT3 are all localized in the chloroplast stroma.
- 日本植物生理学会の論文
著者
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Murata N
National Institute For Basic Biology
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Murata N
National Inst. Basic Biology Okazaki Jpn
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Murata Norio
National Institute For Basic Biology
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Nishida I
Tokyo Univ. Tokyo Jpn
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Nishida Ikuo
Department Of Biochemistry And Molecular Biology Saitama University
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Nishida Ikuo
National Institute For Basic Biology
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Ishizaki Osamu
National Institute For Basic Biology
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Frentzen Margrit
National Institute for Basic Biology
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