The @entity413 transporter @entity1365 was isolated from @entity1 erythrocytes and reconstituted into endogenous membrane lipids. Results from thermal denaturation studies, using differential scanning calorimetry, indicate that the thermal denaturation temperature of @entity1365 is significantly lower in the presence of @entity855 . The lowering of this transition temperature is very dependent on pH. At more acidic pH, @entity855 has a greater effect of lowering the thermal denaturation temperature of the protein. For example, with 4.8 mM @entity855 , the denaturation endotherm is lowered by over 10 degrees at pH 4.3, whereas at pH 7.4, @entity855 does not alter this transition temperature. However, a change in pH alone, in the absence of @entity855 , has very little effect on the denaturation temperature. Both @entity413 and salt partially reverse the lowering of the temperature of thermal denaturation caused by @entity855 . Studies of @entity3323 quenching of the Trp residues of @entity1365 indicate that at neutral pH, @entity855 increases the Stern-Volmer quenching constant, while @entity413 lowers it. The results indicate that @entity855 binds to @entity1365 and destabilizes the native structure, leading to a lowering of the thermal denaturation temperature and an increase in @entity3323 quenching. The effects of @entity855 are reversed in part by @entity413 and are also partly electrostatic in nature.

Ligand-modulation of the stability of the @entity413 transporter XXXX .

@entity1 :: ('9606', 'Species') :: ['human'] @entity3323 :: ('MESH:D020106', 'Chemical') :: ['acrylamide'] @entity1365 :: ('6513', 'Gene') :: ['GLUT 1'] @entity413 :: ('MESH:D005947', 'Chemical') :: ['glucose'] @entity855 :: ('MESH:D000255', 'Chemical') :: ['ATP']
@entity1365 :: (6513,Gene) :: ['GLUT 1']
