Lukash A I, Shepelev A P, Pushkina N V, Tsybul'skiĭ I E, Al'perovich D V
Vopr Med Khim. 1985 Jul-Aug;31(4):104-8.
During incubation of gamma-globulin preparations under conditions similar to physiological ones within 28 days (0.9% NaCl, pH 7.0, 37 degrees) as well as during storage at 3-10 degrees within 36 months gradual nonenzymatic deamidation of the protein occurred mainly due to hydrolysis of readily accessible amide groups (asparagine). Fluorescence of the preparations decreased gradually in the course of deamidation; it constituted for 82% of the initial value after incubation during 28 days. Immunological activity of the gamma-globulin, which lost 19.6% of amide groups, was decreased by 34%; alteration in the amidation by 45.1% was accompanied by a decrease in active antibodies concentration by 92.3%. Nonenzymatic deamidation may be responsible for conformational alterations and inactivation of gamma-globulin.
在28天内于类似于生理条件（0.9%氯化钠、pH 7.0、37摄氏度）下孵育γ-球蛋白制剂的过程中，以及在3至10摄氏度下储存36个月期间，蛋白质逐渐发生非酶促脱酰胺作用，这主要是由于易接近的酰胺基团（天冬酰胺）水解所致。制剂的荧光在脱酰胺过程中逐渐降低；在28天孵育后，其荧光为初始值的82%。失去19.6%酰胺基团的γ-球蛋白的免疫活性降低了34%；酰胺化改变45.1%伴随着活性抗体浓度降低92.3%。非酶促脱酰胺作用可能是γ-球蛋白构象改变和失活的原因。
