OBJECTIVE:To prepare Levofloxacin and triamcinolone acetonide double-loaded ophthalmic gel. METHODS:Us-ing levofloxacin hydrochloride and triamcinolone acetonide as main components,carbopol-940P as base material,HPMC K4M as tackifier,Levofloxacin and triamcinolone acetonide double-loaded ophthalmic gel was prepared. Using dissolution time as index, the contents of carbopol-940P and HPMC K4M were determined by single factor test,and dissolution time,viscosity and the con-tents of 2 main components were also determined. RESULTS:The concentrations of carbopol-940P and HPMC K4M were 0.4%and 1.2%,separately. The dissolution time was more than 24 h and viscosity was 1 142.67 Pa·s. The content of levofloxacin hydro-chloride was 97.3% of labelled amount (RSD=0.84%,n=3),and that of triamcinolone acetonide was 92.97% of labelled amount(RSD=1.32%,n=3). CONCLUSIONS:Levofloxacin and triamcinolone acetonide double-loaded ophthalmic gel has been prepared successfully.

OBJECTIVE: To establish a technical process for the separation and purification of total flavones from Licorice. METHODS: The static absorption capacity of macroreticular adsorptive resins D101、Hz-806、AB-83 for total flavones from licorice were compared. The macroreticular adsorptive resin columns on the Licorice extractives were eluted respectively with different concentrations of ethanol, then the content, the weight of residue and purity coefficient of flavones from Licorice in the eluant were detected. RESULTS: The optimal technological conditions were found in AB-8 as follows: flow rate=3ml/min, sample concentration=1.5 mg/ml, pH=5 and 80% ethanol was used as eluting agent. CONCLUSIONS: AB-8 macroreticular adsorptive resin can effectively separate and purify total flavones from licorice, the purity coefficient thus obtained being over 50%, which meets the requirement of the study of effective components of herbal medicine.

In order to study the functions of the HSPs (Heat shock proteins) of Eimeria tenella, we cloned a novel gene (which designated EtHSP) coding HSP of Eimeria tenella by RT-PCR and RACE (Rapid-amplification of cDNA ends). The full-length cDNA sequence of EtHSP was 1802 bp, containing a 1455 bp ORF (Open reading frame) (GenBank Accession No. FJ911605) encoding a deduced protein of 484 amino acids. Real-time PCR revealed that the mRNA level of EtHSP was much higher in sporozoites of E. tenella than other developmental stages (unsporulated oocysts, sporulated oocysts and merozoites). We constructed the recombinant plasmids pET28a(+)-EtHSP, then transformed it into E. coli BL21(DE3) for expression. SDS-PAGE indicated that the fusion protein was expressed in included bodies, with peak expression 6 h after induction by IPTG Western blotting revealed that the protein was specifically recognized by polyclonal antibodies against E. tenella, showing that the fusion protein was native antigen.
Animals ; Chickens ; Eimeria tenella ; genetics ; metabolism ; Escherichia coli ; genetics ; metabolism ; Heat-Shock Proteins ; genetics ; immunology ; metabolism ; Inclusion Bodies ; metabolism ; Male ; Molecular Sequence Data ; Open Reading Frames ; genetics ; Rabbits ; Recombinant Fusion Proteins ; genetics ; immunology ; metabolism ; Sequence Analysis, Protein