Krichevskaia A A, Lukash A I, Pushkina N V, Sherstnev K B
Vopr Med Khim. 1978 Mar-Apr;24(2):160-3.
gamma-Globulin from human blood serum was incubated in thermostat at 37 degrees within 15, 30, 45, 60 and 72 days. Amount of readily and poorly hydrolyzed amide groups as well as an increase in amino acid content were estimated in the protein at zero time and at these periods. The sterility of the preparation was examined in each case. Spontaneous deamidation of gamma-globulin, observed during incubation, caused an increase in negative charge and altered electrophoretic mobility of the protein molecule. gamma-Globulin was attacked by prothelin more effectively as amount of amide groups was decreased in the protein. Spontaneous deamidation appears to be one of reasons of the protein molecules ageing.
将人血清中的γ-球蛋白在37℃恒温下孵育15、30、45、60和72天。在零时间以及这些时间段对蛋白质中易水解和难水解酰胺基团的量以及氨基酸含量的增加进行了估算。每种情况下都检测了制剂的无菌性。孵育期间观察到的γ-球蛋白的自发脱酰胺作用导致蛋白质分子负电荷增加并改变了电泳迁移率。随着蛋白质中酰胺基团数量的减少，γ-球蛋白受蛋白酶的攻击更有效。自发脱酰胺作用似乎是蛋白质分子老化的原因之一。
