Data in Brief (Dec 2015)

Proteomic and glycomic analyses of a lung-specific protein surfactant protein-D

  • Emi Ito,
  • Ritsuko Oka,
  • Takeo Ishii,
  • Hiroaki Korekane,
  • Ayako Kurimoto,
  • Yasuhiko Kizuka,
  • Shinobu Kitazume,
  • Shigeru Ariki,
  • Motoko Takahashi,
  • Yoshio Kuroki,
  • Kozui Kida,
  • Naoyuki Taniguchi

DOI
https://doi.org/10.1016/j.dib.2015.09.017
Journal volume & issue
Vol. 5, no. C
pp. 707 – 711

Abstract

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In order to verify the protein enriched from pooled human sera to be a lung-specific protein surfactant protein-D (SP-D), we performed peptide mass fingerprinting (PMF)-based protein identification. MASCOT search results of the obtained PMF unequivocally demonstrated that it is identical to human SP-D. Meanwhile, we performed MALDI-QIT-TOF mass spectrometry-based N-glycomic analysis of the recombinant human SP-D produced in murine myeloma cells. The obtained mass spectra of N-glycans from the recombinant SP-D demonstrated that the recombinant protein is almost exclusively modified with core-fucosylated N-glycans [1].