Biochemical and molecular characterization of two phosphatidic acid-selective phospholipase A1s, mPA-PLA1alpha and mPA-PLA1beta.

@article{Hiramatsu2003BiochemicalAM,
  title={Biochemical and molecular characterization of two phosphatidic acid-selective phospholipase A1s, mPA-PLA1alpha and mPA-PLA1beta.},
  author={Tatsufumi Hiramatsu and Hirofumi Sonoda and Yasukazu Takanezawa and R. Morikawa and Mayuko Ishida and Kohji Kasahara and Yutaka Sanai and R. Hakamada Taguchi and Junken Aoki and Hiroyuki Arai},
  journal={The Journal of biological chemistry},
  year={2003},
  volume={278 49},
  pages={
          49438-47
        }
}
We have identified a novel phospholipase A1, named mPA-PLA1beta, which is specifically expressed in human testis and characterized it biochemically together with previously identified mPA-PLA1alpha. The sequence of mPAPLA1beta encodes a 460-amino acid protein containing a lipase domain with significant homology to the previously identified phosphatidic acid (PA)-selective PLA1, mPA-PLA1alpha. mPA-PLA1beta contains a short lid and deleted beta9 loop, which are characteristics of PLA1 molecules… CONTINUE READING

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