Purification of phosphatidylglycerophosphate synthase from Chinese hamster ovary cells

K. Kawasaki, O. Kuge, Y. Yamakawa, M. Nishijima

研究成果: ジャーナルへの寄稿学術誌査読

17 被引用数 (Scopus)

抄録

Phosphatidylglycerophosphate (PGP) synthase catalyses the committed step in the biosynthesis of phosphatidylglycerol and cardiolipin in mammalian cells. Recently we isolated a Chinese hamster ovary (CHO) PGS1 cDNA encoding PGP synthase. In the present study we purified this PGP synthase to near-homogeneity from the mitochondrial fraction of CHO-K1 cells; the final enzyme preparation gave a single 60 kDa protein on SDS/PAGE. Polyclonal antibodies raised against a recombinant CHO PGS1 protein cross-reacted with the purified 60 kDa protein and with CHO membrane proteins of 60 kDa and 62 kDa that increased after transfection with the PGS1 cDNA. The 60 and 62 kDa protein levels in a PGP synthase-defective mutant of CHO-K1 cells were markedly lower than those in CHO-K1 cells. These results indicated that the purified 60 kDa protein was PGP synthase encoded by the PGS1 gene. In addition we found that the purified PGP synthase had no PGP phosphatase activity, indicating that phosphatidylglycerol was produced from CDP-diacylglycerol through two steps catalysed by distinct enzymes, PGP synthase and PGP phosphatase.

本文言語英語
ページ(範囲)9-15
ページ数7
ジャーナルBiochemical Journal
354
1
DOI
出版ステータス出版済み - 2月 15 2001
外部発表はい

!!!All Science Journal Classification (ASJC) codes

  • 生化学
  • 分子生物学
  • 細胞生物学

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