{
  "annotation_id": "7069125b-d039-4643-b3a7-1db716b71ff8",
  "date_created": "2026-03-02T18:01:35.375000Z",
  "date_modified": "2026-03-02T18:01:35.375000Z",
  "file_hash": "a60bdac4270d9dfd194b53bad92ec138052ab46dd33394e2e4479f2fea464632",
  "private": false,
  "record": {
    "abstract": "Membrane and nuclear proteins of poor solubility have been separated by high\nresolution two-dimensional (2-D) gel electrophoresis. Isoelectric focusing with\nimmobilized pH gradients leads to severe quantitative losses of proteins in the\nresulting 2-D map, although the resolution is usually high. Protein solubility\ncould be improved by using denaturing solutions containing various detergents\nand chaotropes. Best results were obtained with a denaturing solution\ncontaining urea, thiourea, and detergents (both nonionic and zwitterionic). The\nusefulness of thiourea-containing denaturing mixtures is shown for microsomal\nand nuclear proteins as well as for tubulin, a protein highly prone to\naggregation.",
    "arxiv_id": "q-bio/0612002",
    "authors": [
      "T. Rabilloud",
      "C. Adessi",
      "A. Giraudel",
      "J. Lunardi"
    ],
    "categories": [
      "q-bio.GN"
    ],
    "doi": "10.1002/elps.1150180303",
    "journal_ref": "Electrophoresis 18 (31/03/1997) 307-16",
    "title": "Improvement of the solubilization of proteins in two-dimensional   electrophoresis with immobilized pH gradients",
    "url": "https://arxiv.org/abs/q-bio/0612002"
  },
  "schema_id": "dorsal/arxiv",
  "source": {
    "execution_id": "d7d46f08-5814-41a4-80f9-309ce0ac7fa1",
    "id": "arXiv Dataset IDs",
    "type": "Model",
    "variant": "snapshot-2026-03-01",
    "version": "0.1.0"
  },
  "user_id": 1000002
}