Isolation and functional characterization of a novel organic solute carrier protein, hOSCP1.

@article{Kobayashi2005IsolationAF,
  title={Isolation and functional characterization of a novel organic solute carrier protein, hOSCP1.},
  author={Yasuna Kobayashi and Akiko Shibusawa and Hironori Saito and Naomi Ohshiro and Masayuki Ohbayashi and Noriko Kohyama and Toshinori Yamamoto},
  journal={The Journal of biological chemistry},
  year={2005},
  volume={280 37},
  pages={32332-9}
}
We succeeded in isolating a novel organic solute carrier from a human placenta cDNA library. The isolated cDNA consisted of 1137 base pairs that encoded a 379-amino acid protein, hOSCP1. Northern blot and reverse transcription PCR analyses revealed that the hOSCP1 mRNA is expressed in the placenta and testis and weakly expressed in the thymus and small intestine. When expressed in Xenopus laevis oocytes, hOSCP1 mediated the high affinity transport of p-aminohippurate (PAH) (K(m) = 35.0 +/- 7.5… CONTINUE READING

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