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

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...

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Detalles Bibliográficos
Autores principales: Ito, Emi, Oka, Ritsuko, Ishii, Takeo, Korekane, Hiroaki, Kurimoto, Ayako, Kizuka, Yasuhiko, Kitazume, Shinobu, Ariki, Shigeru, Takahashi, Motoko, Kuroki, Yoshio, Kida, Kozui, Taniguchi, Naoyuki
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Elsevier 2015
Materias:
Data Article
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4773361/
https://www.ncbi.nlm.nih.gov/pubmed/26958622
http://dx.doi.org/10.1016/j.dib.2015.09.017
Descripción
Sumario: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].

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