| Abstrakt: |
Bovine apo-alpha-lactalbumin was shown to be severalfold more efficient than its calcium conformer as a cofactor in lactose biosynthesis. This rate enhancement was manifested in a 3.5-fold increase in Vmax, with no differences in Km(app) between the two alpha-lactalbumin forms. In the presence of zinc, which shifts Ca(II)-alpha-lactalbumin toward the "apo-like" conformation [Musci, G., & Berliner, L.J. (1985) Biochemistry 24, 3852-3856], the catalytic rate constant for lactose synthesis was identical for both the Ca(II) and apo conformers. Activity measurements at different temperatures, on the other hand, confirmed that calcium is important in stabilizing the protein (alpha-lactalbumin) against thermal denaturation. The stabilizing effect of calcium was independent of the presence of Zn(II), i.e., of the protein conformation. The physiological implications of these results are discussed. |
