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Picodiscs for facile protein-glycolipid interaction analysis.
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- Additional Information
- Source:
Publisher: American Chemical Society Country of Publication: United States NLM ID: 0370536 Publication Model: Print-Electronic Cited Medium: Internet ISSN: 1520-6882 (Electronic) Linking ISSN: 00032700 NLM ISO Abbreviation: Anal Chem Subsets: MEDLINE
- Publication Information:
Original Publication: Washington, American Chemical Society.
- Subject Terms:
- Abstract:
Protein interactions with glycolipids are implicated in diverse cellular processes. However, the study of protein-glycolipid complexes remains a significant experimental challenge. Here, we describe a powerful new assay that combines electrospray ionization mass spectrometry (ESI-MS) and picodiscs, which are composed of human sphingolipid activator protein saposin A and a small number of phospholipids, to display glycolipids in a lipid environment for protein-glycolipid interaction studies in aqueous solution. Time-resolved measurements of enzyme catalyzed hydrolysis of glycolipid substrates and the detection of low, moderate, and high affinity protein-glycolipid interactions serve to demonstrate the reliability and versatility of the assay.
- Grant Information:
Canada Canadian Institutes of Health Research
- Accession Number:
0 (Glycolipids)
0 (Saposins)
EC 3.2.1.18 (Neu3 protein, human)
EC 3.2.1.18 (Neuraminidase)
- Publication Date:
Date Created: 20150325 Date Completed: 20151130 Latest Revision: 20150421
- Publication Date:
20221213
- Accession Number:
10.1021/acs.analchem.5b00170
- Accession Number:
25803566
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