Proteomics

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Arabidopsis thaliana proteome label-free shotgun digested by Legumain in the presence of various denaturants

ABSTRACT: Proteomic optimisation of Arabidopsis thaliana proteome generated using legumain (cleave C-terminal of asparagine/aspartic acid) as protease in the presence of various concentration of denaturants such as acetonitrile, urea, and guanidinium-HCl.

INSTRUMENT(S): maXis

ORGANISM(S): Arabidopsis Thaliana (mouse-ear Cress)

TISSUE(S): Leaf

SUBMITTER: Fatih Demir  

LAB HEAD: Pitter Florian Huesgen

PROVIDER: PXD014699 | Pride | 2020-01-20

REPOSITORIES: Pride

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Publications

ExteNDing Proteome Coverage with Legumain as a Highly Specific Digestion Protease.

Soh Wai Tuck WT   Demir Fatih F   Dall Elfriede E   Perrar Andreas A   Dahms Sven O SO   Kuppusamy Maithreyan M   Brandstetter Hans H   Huesgen Pitter F PF  

Analytical chemistry 20200131 4

Bottom-up mass spectrometry-based proteomics utilizes proteolytic enzymes with well characterized specificities to generate peptides amenable for identification by high-throughput tandem mass spectrometry. Trypsin, which cuts specifically after the basic residues lysine and arginine, is the predominant enzyme used for proteome digestion, although proteases with alternative specificities are required to detect sequences that are not accessible after tryptic digest. Here, we show that the human cy  ...[more]

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