Ziping Yang

TL;DR: This work has used the ability of different lectins to recognize specific glycosylation motifs to develop a specific affinity system that can achieve a comprehensive capture of serum glycoproteins through a multi-lectin affinity column.

TL;DR: M-LAC for isolation of the serum glycoproteome, coupled with liquid chromatography-MS/MS and the use of gene ontology associations, can be used to characterize large panels of candidate markers, which can then be evaluated in a particular patient population.

TL;DR: There was a close correlation between the samples, except for the absence of fibrinogen from the identified‐protein list in the latter sample, which was presumably as a result of the clotting process, and a new system was compared with the previous LCQ platform and gave a greater number of protein identifications, as well as better quality.

TL;DR: The results indicated that the multi-lectin affinity column (M-LAC) is sensitive to changes in the content of sialic acid and fucosyl residues present in serum glycoproteins, and has the potential to be used to screen serum proteins for glycosylation changes due to disease.

TL;DR: A functional annotation of the human plasma proteome was carried out to develop a protein interaction network of proteins identified in this project and addressed several methodological considerations including the selective enrichment of post‐translationally modified proteins by the use of multi‐lectin chromatography and peptidomic techniques to characterize the low molecular weight proteins in plasma.