Through high throughput shotgun proteomics approach, the proteome of seedling leaf of Brassica rapa L. was identified. From three biological replications, a total of 2,122 non-redundant proteins of Brassica rapa L seedling leaf were identified, with a wide range and unbiased physiochemical properties. Their pI values ranged from pH 4.27 (Bra004590) to pH 11.81 (Bra013905). Their molecular weight (MW) ranged from 5.6 kDa (Bra006908) to 534.5 kDa (Bra028068). Gene ontology enrichment analysis revealed that these proteins were associated with cellular process, metabolic process, and enriched catalytic activity compared to whole brassica proteins. The highest presented protein in Brassica rapa seedling leaf was RuBisCO, accounting for 11.56% of total leaf proteins. Also, many ribosomal proteins were identified. The relative amount of all ribosomal proteins comprised 8.47% of total leaf proteins. The relative amount of two RuBisCO and ribosomal proteins was about 20% of total leaf proteins. Thus to detect proteins presenting low abundance, additional fractionating procedure to remove RuBisCO and ribosomal proteins is required.

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Rice anthers from Nipponbare in the flowering stage were collected, proteins extracted and shotgun proteomic analysis conducted. From three biological replications, total 3,198 non-redundant rice anther proteins were identified. There was no bias of physiochemical properties in identified proteins. Proteins showing wide pI value range and molecular weight were identified. The lowest pI value was pH 3.93 (LOC_Os07g41694.1) and the highest was pH 12.48 (LOC_Os01g69020.1). Molecular weights of the identified proteins ranged from 5.2kDa (LOC_Os02g27769.1) to 486.0kDa (LOC_Os09g07300.1). Gene ontolgy enrichment analysis revealed that proteins associated with cellular and metabolic processes, catalytic activity, cell, cell parts, and organelles were enriched in rice anther, suggesting the status of proteins in rice anther were associated with pollen germination and pollen tube elongation. The highly abundant proteins in rice anther were pollen allergens, ATP synthase, glyceraldehyde-3-phosphate dehydrogenase, cupin domain containing proteins, and ascorbate peroxidase.