On the stability of bovine gamma II crystallin.
Bovine gamma II crystallin, undergoes structural changes when lyophilized. The lyophylized powder does not readily dissolve in buffer, although it can be taken up in distilled water. The lyophylized sample, as opposed to a sample concentrated by vacuum distillation at 30 degrees C, does exhibit different migration on isoelectric focusing gels. The hydration and denaturation properties of the two preparations are different. The lyophylized sample possesses a higher non-freezable water content as a function of concentration than its counterpart. The lyophylized sample also shows less denaturation in differential scanning calorimetry scans, up to 110 degrees C, than its counterpart. This indicates that lyophylization may induce a slight denaturation, due to structural-conformational change. On the other hand, the CD spectra of lyophylized and non-lyophylized gamma II crystallins do not differ significantly. This implies that the conformational changes upon lyophylization do not involve the secondary structure of gamma II crystallin.
Bettelheim
F A
FA
Dept. Chemistry, Adelphi University, Garden City, NY 11530.
Reid
M B
MB
McPhie
P
P
Garland
D
D
D000818:Animals; D002152:Calorimetry, Differential Scanning; D002417:Cattle; D002942:Circular Dichroism; D003459:Crystallins / Q000737:chemistry*; D004355:Drug Stability; D005612:Freeze Drying; D007525:Isoelectric Focusing; D011489:Protein Denaturation; D012995:Solubility; D013056:Spectrophotometry, Ultraviolet; D013816:Thermodynamics; D014867:Water / Q000032:analysis
D003459:Crystallins; D014867:Water