Abstract
The in vitro insulin-stimulating action of the trypsinized product of glycinin acidic subunit A1a (A1a/Tr) was examined using rat adipocytes in the presence of bacitracin, chloroquine, colchicine, monensin, and/or Tris, which modifies insulin action in a different manner. The results suggested that A1a/Tr potentiates the insulin-mediated antilipolysis by a similar mechanism to the action of bacitracin, which interferes with extracellular processing of insulin.
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