Title : Abnormal SDS-PAGE migration of cytosolic proteins can identify domains and mechanisms that control surfactant binding.

Pub. Date : 2012 Aug

PMID : 22692797






2 Functional Relationships(s)
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1 By first comparing how 39 amino acid substitutions throughout hSOD1 affected SDS-PAGE migration, we found that substitutions that caused gel shifting occurred within a single polyacidic domain (residues ~80-101), and were nonisoelectric. Sodium Dodecyl Sulfate superoxide dismutase 1 Homo sapiens
2 Capillary electrophoresis, circular dichroism, and size exclusion chromatography demonstrated that amino acid substitutions increase migration during SDS-PAGE by promoting the binding of three to four additional SDS molecules, without significantly altering the secondary structure or Stokes radius of hSOD1-SDS complexes. Sodium Dodecyl Sulfate superoxide dismutase 1 Homo sapiens