RESUMO
Objective To provide clinical experience in treatment of cook′s fungus infection of evidence‐based medical evidence , separation of medical environment of cook′s bacteria identification and antimicrobial susceptibility test .Methods Collected in the hospital infection of hygiene monitoring ,collection and medical staff hands ,skin and mucous membrane ,air and object surface sam‐ples from 86 strains of cook ,application ATB Expression semi‐automatic bacteria identification of susceptibility analyzer supporting article try ID32 Staph identification and drug susceptibility test Staph 5 ,strain identification and drug sensitive test .Results 86 strains bacteria identification cook 62 strains bacteria ,mutation detection rose cook bacteria strains of 16 ,cook eight strains of bac‐teria .Cook bacterium of norfloxacin(16 .3% ) ,and with nitrofurantoin low because of the sensitive rate(20 .9% ) ,of erythromycin (69 .3% ) and gentamycin(67 .4% ) ,the sensitive rate at nearly 70 .0% ,sensitivity to penicillin and other 12 kinds of antimicrobial a‐gents more than 80 .0% ,even 100 .0% .Conclusion Cook for most still sensitive ,clinicians and microorganism inspection personnel should strengthen the cook .
RESUMO
The interaction of patulin with human serum albumin (HSA) was studied in vitro under normal physiological conditions. The study was performed using fluorescence, ultraviolet-visible spectroscopy (UV-Vis), circular dichroism (CD), atomic force microscopy (AFM), and molecular modeling techniques. The quenching mechanism was investigated using the association constants, the number of binding sites, and basic thermodynamic parameters. A dynamic quenching mechanism occurred between HSA and patulin, and the binding constants (K) were 2.60 × 10(4), 4.59 × 10(4), and 7.01 × 10(4) M(-1) at 288, 300, and 310 K, respectively. Based on fluorescence resonance energy transfer, the distance between the HSA and patulin was determined to be 2.847 nm. The ΔG (0), ΔH (0), and ΔS (0) values across various temperatures indicated that hydrophobic interaction was the predominant binding force. The UV-Vis and CD results confirmed that the secondary structure of HSA was altered in the presence of patulin. The AFM results revealed that the individual HSA molecule dimensions were larger after interaction with patulin. In addition, molecular modeling showed that the patulin-HSA complex was stabilized by hydrophobic and hydrogen bond forces. The study results suggested that a weak intermolecular interaction occurred between patulin and HSA. Overall, the results are potentially useful for elucidating the toxigenicity of patulin when it is combined with the biomolecular function effect, transmembrane transport, toxicological, testing and other experiments.
