Effect of Glycine on pH Changes and Protein Stability During Freeze–Thawing in Phosphate Buffer Systems

Solute Crystallization in Mannitol–Glycine Systems—Implications on Protein Stabilization in Freeze‐Dried Formulations

“…Similar observations were made by Pikal-Cleland et al, 20 who reported that at low glycine concentrations, the crystallization of sodium and potassium phosphate buffer salts were inhibited during cooling possibly due to a decrease in the nucleation rate. 20 Additionally, when we studied the same system at slower cooling rates (28C/min), both the solutes crystallized at glycine concentrations !1% w/w (data not shown). These results indicate that in frozen aqueous solutions, glycine had a stronger tendency to crystallize than mannitol.…”

Lead bioaccessibility in 12 contaminated soils from China: Correlation to lead relative bioavailability and lead in different fractions

“…S2B). The increased Pbbioaccessibility with glycine was probably related to its strong pH buffering ability [35]. We observed that more HCl (290 L) was needed to adjust 20 mL of glycine solution to pH 1.5 than thoseneeded for adjusting pepsin and mucin solution (80 and 105 L) and Milli-Q water (70 L).…”

Protein aggregation: Pathways, induction factors and analysis

“…53 These effects are regarded as possible causes of freezing-induced protein denaturation and aggregation. The freezing rate as well as the method and control of thawing has been previously reported to influence the rate of protein aggregation.…”