{
  "annotation_id": "4636c216-d30f-4fb4-974f-981e09b33c47",
  "date_created": "2026-03-02T18:01:31.152000Z",
  "date_modified": "2026-03-02T18:01:31.152000Z",
  "file_hash": "1ab264064b3e70bb628fef313130b2caa5f4881aabe583cbba84e090609a17b8",
  "private": false,
  "record": {
    "abstract": "Preparations of arachidonic acid binding and non-binding proteins from bovine\nbrain, four acidic proteins (alpha-casein, phosvitin, beta-lactoglobulin A and\nB), the peptide polyglutamate, and two polyanions (heparin, dextran sulfate)\nenhanced both basal and glucose 6-phosphate induced solubilization of rat brain\nmitochondrial hexokinase (ATP:D-hexose 6-phosphotransferase, EC 2.7.1.1). In\ncontrast, three other acidic proteins, had little (alpha-lactalbumin) or no\neffect (bovine serum albumin, ovalbumin) and five basic proteins inhibited\nrelease of the enzyme. Solubilizing activity therefore appears to require a net\nnegative charge and one or more of the following structural features: extended\nconformation, random coil, and unordered or beta-structure, in the latter case,\nas the beta-barrel in the fatty acid binding proteins and beta-lactoglobulins.\nIt is of interest that a difference of a single negative charge between\nbeta-lactoglobulin A and B, resulted in a statistically significant difference\nin the stimulation of hexokinase release. Possible physiological and\npathological roles of this hexokinase solubilizing effect are discussed\nbriefly.",
    "arxiv_id": "q-bio/0502028",
    "authors": [
      "F. Moller"
    ],
    "categories": [
      "q-bio.BM",
      "q-bio.SC"
    ],
    "title": "Release of Brain Mitochondrial Hexokinase by Acidic Proteins and   Macromolecular Polyanions",
    "url": "https://arxiv.org/abs/q-bio/0502028"
  },
  "schema_id": "dorsal/arxiv",
  "source": {
    "execution_id": "9ec964e2-011d-4f61-8fd3-59d457aa6f92",
    "id": "arXiv Dataset IDs",
    "type": "Model",
    "variant": "snapshot-2026-03-01",
    "version": "0.1.0"
  },
  "user_id": 1000002
}