title: Aggregation of binding protein from rat nerve.
abstract: Leucine-binding protein described in an earlier paper was examined to characterize the dynamic properties of the system. Leucine-binding protein assembles into a large protein polymer or complex (greater than 302,000 daltons). Colchicine reduces and Mg2+ increases the amount of polymer formed. Trypsin destroys the isolated polymer but RNAase and collagenase do not. Mg2+-ATPase activity is present in the polymer fraction. The formation of the large complex suggests a quickly adaptable structure capable of responding to ionic and environmental conditions.
mesh_terms: D000818:Animals; D002352:Carrier Proteins / Q000378:metabolism; D003078:Colchicine; D007930:Leucine / Q000378:metabolism; D046911:Macromolecular Substances; D008274:Magnesium; D008970:Molecular Weight; D009419:Nerve Tissue Proteins / Q000378:metabolism; D009474:Neurons / Q000378:metabolism*; D011485:Protein Binding; D051381:Rats; D014357:Trypsin
chemical_list: D002352:Carrier Proteins; D046911:Macromolecular Substances; D009419:Nerve Tissue Proteins; D014357:Trypsin; D007930:Leucine; D008274:Magnesium; D003078:Colchicine