| Article ID | Journal | Published Year | Pages | File Type |
|---|---|---|---|---|
| 10797942 | Biochimica et Biophysica Acta (BBA) - Biomembranes | 2011 | 7 Pages |
Abstract
âºCLS protein (C-terminal fragment of L-selectin, residues S473-R542) exhibits anomalously slow electrophoretic rate in SDS-PAGE. âºBasic-rich juxtamembrane region is responsible for the slow migration in SDS gel. âºCLS is monomeric in zwitterionic detergent micelles by FRET. âºL-selectin transmembrane domain lacks propensity to dimerize in a cell membrane.
Keywords
tetramethylrhodamineTOXCATL-selectinPSGL-1DPChexafluoroisopropanolHFIPGSTTMRCATSDS-PAGESodium dodecyl sulfate polyacrylamide gel electrophoresisFluorescence resonance energy transferFRETTris(2-carboxyethyl) phosphine hydrochloridetransmembrane domainDodecylphosphocholinecircular dichroismtransmembraneP-selectin glycoprotein ligand-1Membrane proteinhigh performance liquid chromatographyHPLCchloramphenicol acetyl transferaseglutathione S-transferase
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Authors
Sankaranarayanan Srinivasan, Wei Deng, Renhao Li,