e-journal

Isotope Targeted Glycoproteomics (IsoTaG) to Characterize Intact, Metabolically Labeled Glycopeptides from Complex Proteomes

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Protein glycosylation plays many critical roles in biological function and creates the most diversity of all post-translational modifications (PTMs). Glycan structural diversity is directly correlated with difficulty in characterizing the intact glycoproteome by mass spectrometry (MS). In this protocol, we describe a novel mass-independent chemical glycoproteomics platform for characterizing intact, metabolically labeled glycopeptides from complex proteomes, termed Isotope Targeted Glycoproteomics (IsoTaG). To use IsoTaG, cell culture samples
are metabolically labeled with an azido- or alkynyl-sugar. Metabolically labeled glycoproteins are then tagged using Click chemistry and enriched with an isotopic recoding biotin probe. Intact glycopeptides are recovered by cleavage of the probe, analyzed with directed MS, and assigned by targeted massindependent data analysis. The outlined procedure is well defined in cell culture and has been executed with over 15 cell lines.

Keywords: glycoproteomics  bioorthogonal chemistry  metabolic labeling  chemical proteomics  mass spectrometry

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Ketersediaan

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Informasi Detail

Judul Seri

Current Protocols in Chemical Biology

No. Panggil

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Penerbit

Malden, USA : John Wiley & Sons, Inc.., 2016

Deskripsi Fisik

Curr. Protoc. Chem. Biol. 8:59-82.

Bahasa

English

ISBN/ISSN

doi: 10.1002/9780470

Klasifikasi

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Tipe Isi

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Tipe Media

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Tipe Pembawa

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Edisi

8: March 2016

Subjek

KIMIA

Info Detail Spesifik

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Pernyataan Tanggungjawab

agus

Versi lain/terkait

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