Rat liver membrane glycoproteome: enrichment by phase partitioning and glycoprotein capture

Journal of Proteome Research
Albert LeeNicolle H Packer

Abstract

Past proteomic studies of membrane proteins have often been hampered by the low abundance and relatively high hydrophobicity of these proteins. Proteins are often glycosylated, particularly on the extracellular surface of the plasma membrane, and this characteristic was targeted as an enrichment strategy for identifying membrane proteins. Here, we report a strategy for identifying the tissue membrane glycoproteome, which involves (1) Triton X-114 phase partitioning, (2) isolation of glycosylphosphatidylinositol (GPI)-anchored proteins, and (3) glycoprotein capture using lectin affinity or hydrazine chemistry. Surprisingly, the capture of membrane proteins by lectin affinity and hydrazine chemistry resulted in mostly different populations of enriched glycoproteins. Lectins enriched high molecular weight functional membrane proteins with more potential glycosylation such as those involved in signal transduction and cell adhesion. Conversely, hydrazine chemistry isolated a higher proportion of smaller, enzymatic and peripheral membrane proteins such as solute carrier transporters and cytochrome p450s. We have applied our strategy to characterize the rat liver membrane glycoproteome and identified four new predicted GPI-anchored pr...Continue Reading

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Citations

Jun 9, 2012·Nature Protocols·Daniel KolarichNicolle H Packer
Jun 9, 2012·Nature Protocols·Pia H JensenNicolle H Packer
Aug 24, 2011·Molecular & Cellular Proteomics : MCP·Miyako NakanoNicolle H Packer
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Feb 22, 2017·Laboratory Investigation; a Journal of Technical Methods and Pathology·Hongjiao CaiLi Jia
Jul 21, 2021·Biochemical Society Transactions·Tiago OliveiraDaniel Kolarich

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