Vibrational sum frequency generation (VSFG) spectroscopy and surface pressure measurements are used to investigate the adsorption of a globular protein, bovine serum albumin (BSA), at the air/water interface with and without the presence of salts. We find at low (2 to 5 ppm) protein concentrations, which is relevant to environmental conditions, both VSFG and surface pressure measurements of BSA behave drastically different from at higher concentrations. Instead of emerging to the surface immediately, as observed at 1000 ppm, protein adsorption kinetics is on the order of tens of minutes at lower concentrations. Most importantly, salts strongly enhance the presence of BSA at the interface. This "salting up" effect differs from the well-known "salting out" effect as it occurs at protein concentrations well-below where "salting out" occurs. The dependence on salt concentration suggests this effect relates to a large extent electrostatic interactions and volume exclusion. Additionally, results from other proteins and the pH dependence of the kinetics indicate that salting up depends on the flexibility of proteins. This initial report demonstrates "salting up" as a new type of salt-driven interfacial phenomenon, which is worthy of continued investigation given the importance of salts in biological and environmental aqueous systems.