1.Failure Causes Analyses and Corrective Actions of Two Different Types of Bowie-Dick Test Pack
Riqing LIN ; Lihua DENG ; Yunfang MA ; Jinzhu LIU
Chinese Journal of Nosocomiology 2005;0(11):-
OBJECTIVE To analyze the monitoring performance and testing efficacy and reliability of standardized disposable B-D test pack and standard linen test pack,and summarize the corrective actions based on failure analyses for future reference.METHODS The two different test packs were employed to evaluate the vacuum performance of dynamic air removal sterilizer.RESULTS We enrolled 400 standardized disposable B-D test packs and standard linen test packs respectively.The disposable pack failed 4 cases with the success ratio 99%,while the linen pack failed 30 cases with the success ratio 92.5%.CONCLUSIONS The poor conformity of hand-made linen test pack,variation of steam pressure,sterilizer failure,and unprofessionalism of sterilizer operator contribute as main failure causes in B-D test.Standardized disposable B-D test pack can decrease subjective factors significantly,and the test results are more reliable and standardized.
2.Hemolytic Effects of Melittin Involve Activity Change of Two Types of Enzymes on RBC Membrane
Yahua ZHAO ; Riqing LI ; Wei ZHANG ; Yangsheng ZHONG ; Zucheng LIANG ; Jianrong LIN
Chinese Journal of Biochemistry and Molecular Biology 2008;24(6):522-530
The effects of melittin on the activities of Na+-K+-ATPase and glucose-6-phosphate dehydrogenase (G-6-PD) which are on the membrane of red blood cell (RBC) are chosen as the index of this study. The possible target sites of these effects through enzyme activity determination by spectrophotometry are investigated, and the hemolytic process and the activity change of these two types of enzymes on the RBC membrane are discussed. The results show that the main mode of melittin inhibition to the activity of enzymes on the RBC membrane is the coexistence of adhesion/insertion form and free-state form, and the effect of the former is more stronger than the latter. The K+ binding site of Na+-K+-ATPase is one of the target sites of melittin. The membrane-insertion process of melittin synchronizes with the action of melittin on this enzyme. Melittin slowly inhibits the catalysis of G-6-PD through the action on G-6-P and NADP, and the extent in which melittin forms tetramers isclosely related to the enzyme activity. EDTA inhibits the aggregation of melittin, and interferes with its action on G-6-P. The biochemical mechanisms of melittin effects on the substrate G-6-P and the coenzyme NADP are similar, and the inhibition of melittin is not related to the structure of G-6-PD.