Gu J X, Matsuda T, Nakamura R, Ishiguro H, Ohkubo I, Sasaki M, Takahashi N
Department of Food Science and Technology, School of Agriculture, Nagoya University, Aichi.
J Biochem. 1989 Jul;106(1):66-70. doi: 10.1093/oxfordjournals.jbchem.a122821.
Hen ovomucoid was chemically deglycosylated by treatment with trifluoromethanesulfonic acid at 0 degrees C for 60 min. About 75 mol% of the carbohydrate moiety was removed from the glycoprotein without changing its amino acid composition, and its trypsin inhibitory activity and immunoreactivity with specific antibodies remained unchanged. The deglycosylated ovomucoid was inactivated and degraded easily by an excess amount of trypsin, whereas the native glycoprotein was not. Furthermore, the biological and immunological activities of the deglycosylated ovomucoid were lowered by heat treatment more easily than those of the native ovomucoid. These results suggest that the carbohydrate moiety of ovomucoid contributes to the stability of the ovomucoid molecule against tryptic hydrolysis and heat denaturation.
通过在0℃下用三氟甲磺酸处理60分钟,对鸡蛋类黏蛋白进行化学去糖基化。从糖蛋白中去除了约75摩尔%的碳水化合物部分,而其氨基酸组成未发生变化,并且其胰蛋白酶抑制活性和与特异性抗体的免疫反应性保持不变。去糖基化的类黏蛋白很容易被过量的胰蛋白酶灭活和降解,而天然糖蛋白则不会。此外,与天然类黏蛋白相比,去糖基化的类黏蛋白经热处理后其生物学和免疫学活性更容易降低。这些结果表明,类黏蛋白的碳水化合物部分有助于类黏蛋白分子抵抗胰蛋白酶水解和热变性的稳定性。