Abstract
1. 1.|Hydrogen-bonding of NH 4 + to bovine serum albumin and bovine and equine α-globulins was detected by infrared spectroscopy. NH 4 + caused perturbations of the NH stretching mode at 3300 cm −1 of films of proteins cast from solutions of NH 4Cl. Mixing of KCl with NH 4Cl reduced the perturbation. 2. 2.|The interaction of NH 4 + with α-globulins caused them to lose stability to heating. The specific viscosity of solutions of bovine serum albumin was decreased by NH 4Cl or KCl but was increased by NaCl, acetate salts, or urea at high concentrations. The extent of tryptic digestion of bovine serum albumin was decreased in NH 4Cl solutions but increased in 6 M urea solutions in comparison to distilled water.
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