Day D F, Ingram J M
Can J Microbiol. 1981 May;27(5):531-5. doi: 10.1139/m81-078.
Glutaraldehyde, the biological fixative of choice in the cytochemical localization of the phosphatases, was investigated for its effects on Pseudomonas aeruginosa alkaline phosphatase. Comparative studies on the inactivation of alkaline phosphatase by glutaraldehyde showed significant differences when the purified protein was compared with whole, cell-bound enzyme. The effects of the reagent on the kinetics of the purified enzyme were studied and some conclusions drawn as to the mode of inactivation. The reaction of glutaraldehyde with the cell envelope of P. aeruginosa was also investigated, and it was found not to modify the extraction of lipopolysaccharides from the outer membrane. This study emphasizes the care that must be taken to interpret data, cytochemical or otherwise, obtained when glutaraldehyde is used as a fixative or cross-linking reagent.
戊二醛是磷酸酶细胞化学定位中首选的生物固定剂，本研究考察了其对铜绿假单胞菌碱性磷酸酶的影响。戊二醛使碱性磷酸酶失活的对比研究表明，当将纯化的蛋白质与完整的、细胞结合的酶进行比较时，存在显著差异。研究了该试剂对纯化酶动力学的影响，并就失活模式得出了一些结论。还研究了戊二醛与铜绿假单胞菌细胞包膜的反应，发现它不会改变从外膜提取脂多糖的情况。本研究强调，在解释使用戊二醛作为固定剂或交联剂时获得的细胞化学或其他数据时必须谨慎。
