Sakane F, Takahashi K, Takayama H, Koyama J
Department of Hygienic Chemistry, Faculty of Pharmaceutical Sciences, Hokkaido University.
J Biochem. 1987 Aug;102(2):247-53. doi: 10.1093/oxfordjournals.jbchem.a122048.
The membrane fraction of guinea pig polymorphonuclear leukocytes stimulated with phorbol myristate acetate exhibits the respiratory burst NADPH oxidase activity. This activity is markedly unstable at 37 degrees C, disappearing with a half-life of 11.0 min. When the membrane fraction was pretreated with 0.1% glutaraldehyde, the NADPH oxidase was found to become more stable; its half-life increased about sixfold without any enhancement of the initial activity. The glutaraldehyde treatment of the membrane fraction also protected the NADPH oxidase against inactivation with 0.1-0.2% Triton X-100. These stabilizing effects of glutaraldehyde on the NADPH oxidase seem to be due to its protein cross-linking ability, since its monovalent analogue, butyraldehyde, did not show any effect on the NADPH oxidase activity. In fact, sodium dodecyl sulfate-polyacrylamide gel electrophoresis revealed that glutaraldehyde cross-linked many proteins constituting the membrane.
用佛波醇肉豆蔻酸酯乙酸盐刺激豚鼠多形核白细胞的膜部分，表现出呼吸爆发NADPH氧化酶活性。该活性在37℃时明显不稳定，以11.0分钟的半衰期消失。当膜部分用0.1%戊二醛预处理时，发现NADPH氧化酶变得更稳定；其半衰期增加了约六倍，而初始活性没有任何增强。膜部分的戊二醛处理也保护NADPH氧化酶不被0.1 - 0.2% Triton X - 100灭活。戊二醛对NADPH氧化酶的这些稳定作用似乎归因于其蛋白质交联能力，因为其单价类似物丁醛对NADPH氧化酶活性没有任何影响。事实上，十二烷基硫酸钠 - 聚丙烯酰胺凝胶电泳显示戊二醛交联了构成膜的许多蛋白质。
