Polarized antiquark flavor asymmetry in Drell-Yan pair production

咖啡酸类似物合成的研究进展
李冰菲;张悦;孟丹
【期刊名称】《黑龙江医药》
【年(卷),期】2013(000)006
【摘要】咖啡酸苯乙酯（CAPE）是蜂胶中的主要成分之一，具有很好的抗炎症性和抗氧化作用[1,2]，抗病毒，抗菌，消炎，抗动脉硬化，抑制DNA，诱导细胞凋亡及免疫调节等药理活性。

本文主要介绍总结咖啡酸苯乙酯及其衍生物的药理活性及其合成方法的研究。

【总页数】3页(P1037-1038,1039)
【作者】李冰菲;张悦;孟丹
【作者单位】黑龙江中医药大学黑龙江，哈尔滨，150040;黑龙江省智诚医药科技有限公司;黑龙江中医药大学黑龙江，哈尔滨，150040
【正文语种】中文
【中图分类】TQ463
【相关文献】
1.咖啡酸衍生物的合成方法及其生物活性研究进展 [J], 曾方;陈友宝;夏春年;钟光祥
2.咖啡酸酯类和酰胺类衍生物的合成和应用研究进展 [J], 曹敏;归萌;同婉莹;余丽丽
3.蜂胶中咖啡酸苯乙酯的合成及应用研究进展 [J], 张梅梅;谢英花;刘朝霞;张冬梅
4.木质素生物合成关键酶咖啡酸-O-甲基转移酶基因(COMT)的研究进展 [J], 李波;
倪志勇;王娟;吕萌;范玲
5.咖啡酸苯乙酯的合成研究进展 [J], 卢定强;蒋奔;王俊;赵辉;凌岫泉;刘骥
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Product InformationMonoclonal ANTI-FLAG® M2, Clone M2 Produced in Mouse, Affinity Isolated AntibodyF1804Storage Temperature −20 °CProduct DescriptionMonoclonal ANTI-FLAG® M2 is a mouse-derived, affinity-purified IgG1 monoclonal antibody that binds to fusion proteins containing a FLAG® peptide sequence.1 The M2 antibody will recognize a FLAG® peptide sequence at the N-terminus,Met-N-terminus, C-terminus, or internal sites of a fusion protein. Binding of the M2 antibody is not dependent on calcium.Monoclonal ANTI-FLAG® M2 is useful for detection, identification, and capture of fusion proteins that contain a FLAG® peptide sequence by common immunological procedures, such as Western blotting, immunofluorescence, and immunoprecipitation. ReagentSupplied at a concentration of ∼ 1 mg of protein per mL of solution, and formulated in 50% glycerol,10 mM sodium phosphate, and 150 mM NaCl,pH 7.4. The formulation contains no antimicrobial preservatives.Antigenic binding siteN-Asp-Tyr-Lys-Asp-Asp-Asp-Asp-Lys-C SpecificityThe monoclonal antibody detects only the target protein band(s) on a Western blot from an E. coli, plant or mammalian crude cell lysate.SensitivityThe monoclonal antibody detects as little as 2 ng of target protein by dot blot. The Western blot is tested down to 10 ng, but may detect lower using the procedure detailed below. Precautions and DisclaimerFor R&D use only. Not for drug, household,or other uses. Please consult the Safety Data Sheet for information regarding hazards and safe handling practices.Preparation InstructionsImmediately prior to use, dilute the monoclonal antibody in Tris-buffered saline (TBS), pH 8.0, with 3% nonfat milk (Cat. No. T8793). Dilutions in the described procedures are provided as guidelines. Adjust the antibody concentration to maximize detection sensitivity and minimize background. StorageStore the undiluted antibody at −20 °C in working aliquots. The product, as formulated, will not freeze when stored at the recommended temperature. Note: Over time, small amounts of purified antibodies can precipitate due to intermolecular hydrophobic interactions. If precipitate is observed in this product, briefly centrifuge the vial to pellet the precipitate. Withdraw the desired volume of antibody solution from the clear supernatant for use. This should not alter the performance of the purified antibody in most applications.ProceduresWestern Blot Immunostaining2-5Note: this procedure is based on chemiluminescent detection using Chemiluminescent Peroxidase Substrate-1 (Cat. No. CPS160). Dilutions of both primary and secondary antibodies may require optimization when using other substratesor conditions.1.Separate fusion proteins containing aFLAG® peptide sequence from sample lysatesusing a standard SDS-PAGE protocol. Load2.5–10 µg of total protein lysate per lane.2.Transfer proteins from the gel to a nitrocellulosemembrane, Immobilon®-P, or otherpolyvinylidene difluoride (PVDF) membrane. ThePVDF membrane may provide greaterdownstream sensitivity.3.Wash the blot in at least 0.5 mL/cm2 of purifiedwater for 2–3 minutes employing gentle agitation (50–60 rpm).4.Block the blot with at least 0.5 mL/cm2 ofTris Buffered Saline (TBS), pH 8.0, with 3%nonfat milk for 30 minutes at room temperature, employing gentle agitation.5.Remove the blocking agent and wash once with0.5 mL/cm2 of Tris buffered saline, pH 8.0(Cat. No. T6664).6.Add the desired concentration of monoclonalantibody to the blot. A final antibodyconcentration of 1 µg/mL (1:1,000 dilution of the antibody as supplied) in at least 0.5 mL/cm2 ofTBS with 3% nonfat milk is suggested. Incubateat room temperature for 30 minutes employinggentle agitation.Note: Dilutions must be optimized for differentsubstrates and systems.7.Decant off the Monoclonal ANTI-FLAG® M2solution and wash once with at least 0.5 mL/cm2of TBS, pH 8.0.8.Add the secondary antibody in the form ofAnti-Mouse IgG-Peroxidase (Cat. No. A9044) orequivalent. The concentration of secondaryantibody must be optimized based on thesubstrate being used. For detection usingChemiluminescent Peroxidase Substrate-1, a final secondary antibody dilution of 1:30,000 should be employed. Specifically, it is suggested theantibody as supplied be diluted in at least0.5 mL/cm2 of TBS with 3% nonfat milk. Incubatethe blot employing gentle agitation at roomtemperature for 30 minutes. 9.Wash the blot at least three times for a total of15 minutes (5 minutes per wash) in TBS with0.05% TWEEN® 20, pH 8.0 (Cat. No. T9039).Agitate gently, employing at least 0.5 mL/cm2 ofwash solution.10.Develop the blot using ChemiluminescentPeroxidase Substrate-1 or an equivalent reagentfor 5 minutes. Do not agitate the blot during this incubation step. Drain briefly and wrap inplastic film.11.Expose BioMax® Light film to the blot for a rangeof times from several seconds up to 10 minutes.It is recommended that a quick exposure of10–30 seconds be performed to determine theoptimal exposure time needed. If the signal is too intense even at the short exposure times, allowthe signal to decay over a 1–8 hour period(or longer if necessary), and then re-exposethe film.Indirect ImmunofluorescentCytochemical StainingMonoclonal ANTI-FLAG® M2 may be utilized in immunocytochemical staining procedures when used in conjunction with a labeled secondary antibody (indirect).6 A generic procedure for adherent cell staining is described, using immunofluorescence, employing an Anti-Mouse IgG-FITC conjugate asthe label.1.Grow and transfect cells on coverslips.2.Fix the cells by incubation with phosphatebuffered saline, pH 7.4 (Cat. No. P3813),containing 4% paraformaldehyde (Cat. No.P6148), and 4% sucrose (Cat. No. S1888) for15 minutes at room temperature.3.Wash the fixed cells with PBS for 5 minutes.Repeat once.4.Permeabilize the cells by incubation with 0.25%TRITON™ X-100 (Cat. No. T9284) in PBS for5 minutes.5.Wash the cells with PBS for 5 minutes.Repeat once.6.Block by incubation with 10% bovine serumalbumin (Cat. No. A9647) in PBS (10% BSA/PBS) for 30 minutes at 37 °C.7.Incubate with Monoclonal ANTI-FLAG® M2 dilutedin the range of 1:500 to 1:2,000 in 3% BSA/PBSfor 2 hours at 37 °C.8.Wash with PBS for 5 minutes. Repeat twice.9.Incubate with the secondary antibody, Anti-MouseIgG- FITC (Cat. No. F9137) at a 1:1,000 dilutionin 3% BSA/PBS for 45 minutes at 37 °C.10.Wash with PBS for 5 minutes. Repeat twice.11.Mount coverslips with cells side down on glassslides using a small drop of mounting mediumsuch as polyvinyl alcohol for semi-permanentmounting. The inclusion of an anti-fading agentlike DABCO® in the mounting medium(25–100 mg/mL, for example Cat. No. 10981) isstrongly recommended. Seal coverslips to glassslides (with nail polish, for instance).12.Examine by fluorescence microscopy. FITC has anabsorption maximum at 492 nm with an emission maximum at 520 nm. Immunoprecipitation (IP)Monoclonal ANTI-FLAG® M2 may be used in IP procedures when used in conjunction with an insoluble carrier matrix, such as a Protein G resin. Alternatively, EZview™ Red Protein G Affinity Gel (Cat. No. E3403) or the Protein G Immunoprecipitation Kit (Cat. No. IP50) may be used. EZview Red ANTI-FLAG® M2 Affinity Gel(Cat. No. F2426) or ANTI-FLAG® M2 Affinity Gel (Cat. No. A2220) may be utilized directly for IP. See reference 5 for general protocols.Enzyme Immunoassay (EIA)Monoclonal ANTI-FLAG® M2 may be used in EIA procedures. Typically, a fusion protein containing a FLAG® peptide sequence is directly adsorbed (or otherwise presented) within the wells of a multiwell polystyrene plate. The Monoclonal ANTI-FLAG® M2 antibody may be diluted up to 1:50,000 for subsequent incubation within the plate wells. Detection may be accomplished using Anti-Mouse IgG-Peroxidase (Cat. No. A9044) or equivalent, diluted 1:10,000, followed by an appropriate substrate for visualization.We also offer the ANTI-FLAG® High Sensitivity, M2 coated 96-well plate (Cat. No. P2983) for EIA-based screening applications. References1.Brizzard, B.L., et al., Immunoaffinity purificationof FLAG® epitope-tagged bacterial alkalinephosphatase using a novel monoclonal antibodyand peptide elution. BioTechniques, 16(4):730-735 (1994).2.Bjerrum, O.J., and Heegaard. N.H.H., CRCHandbook of Immunoblotting of Proteins, Volume I, Technical Descriptions. CRC Press(Boca Raton, FL), pp. 229-236 (1988).3.Dunbar, B.S. (ed.), Protein Blotting: A PracticalApproach. IRL Press (New York, NY),pp. 67-70 (1994).4.Fortin, A., et al., A 56- to 54-kilodalton non gratasignal in immunoblot analysis using thehorseradish peroxidase chemiluminescencesystem. Biochem. Cell Biol., 72(5-6):239-243 (1994).5.Harlow, E., and Lane, D., Antibodies: ALaboratory Manual. Cold Spring Harbor Laboratory Press (Cold Spring Harbor, NY) (1988).6.Ciaccia, A.V., and Price, E.M., IBI FLAG Epitope,1: 4-5 (1992)..Troubleshooting Guide (Western Blot Immunostaining Procedure) Problem Possible Cause SolutionFusion protein is not detected. Protein is notexpressed.Verify nucleic acid sequence and reading frame of the FLAG® fusionprotein in vector construct. If sequence is present, attempt tooptimize expression.Target proteinpoorly representedin sample.Positive controls (10 ng/lane recommended) should always beincluded. If the positive control works, the sample may not containthe FLAG® fusion protein of interest, or it may be present atconcentrations too low to detect. Immuno-precipitation withANTI-FLAG® M2 Affinity Gel (Cat. No. A2220) may be required forlow concentrations of FLAG fusion proteins.Positive controls we have available:•Amino-terminal FLAG-BAP™ Fusion Protein (Cat. No. P7582).•Carboxy-terminal FLAG-BAP™ Fusion Protein (Cat. No. P7457).•Amino-terminal Met-FLAG-BAP™ Fusion Protein (Cat. No. P5975).Defective detectionreagentsRun appropriate controls to ensure performance. Use 10 ng/lane of acontrol FLAG-BAP™-fusion protein as a positive control. If no signal isobtained with the control, repeat the procedure using a fresh lot ofsecondary antibody-HRP conjugate, along with freshly preparedreagents.Inadequateexposure timeusingchemiluminescentsystem.If no signal is observed on the film, expose for longer times. It isrecommended to try exposure times ranging from about 5 seconds toas long as 10 minutes.Inappropriate film Switch to film designated for chemiluminescent detection such asBioMax® Light.No target proteinpresent onmembrane.Verify transfer onto the membrane by visualizing proteins usingPonceau S solution (Cat. No. P7170). If possible, a positive controlshould always be run to ensure that the detection systemcomponents are functioning normally. Pre-stained protein markers(for example, Cat. No. C1992 or C4861) may also be used to verifycomplete transfer of proteins from gel to membrane.Antigen is coveredby blockingreagent, due tooverblocking.Masking of a signal can occur if the blocking reagent (such as caseinor gelatin containing blocking buffers) is used at an excessively highconcentration. A dilution ranging from 1:1 to 1:3 may be performedto decrease the concentration of blocking reagent. If the problempersists, use TBS with 3% nonfat milk (Cat. No. T8793).Antibodyconcentration isnot optimal.Determine the optimal working dilution for the MonoclonalANTI-FLAG® M2 antibody via titration. Consider using a higherconcentration of antibody, if no signal or a weak signal is detected.Also, antibody used at an excessively high concentration can causesignal inhibition, especially in chemiluminescent detection systems.The life science business of Merck operatesas MilliporeSigma in the U.S. and Canada.Merck and Sigma-Aldrich are trademarks of Merck KGaA, Darmstadt, Germany or its affiliates.All other trademarks are the property of their respective owners. Detailed information on trademarks is available via publicly accessible resources.Problem Possible Cause SolutionHigh non-specific background Cellular extract concentration istoo high.2.5–10 µg of total lysate protein perlane is usually enough to obtain agood signal. Load less cellularextract or serially dilute the cellularextract to determine the optimalsignal to noise ratio.Monoclonal ANTI-FLAG® M2antibody concentration is too high.Dilute the Monoclonal ANTI-FLAG®M2 antibody to a concentrationranging from 0.1–0.5 µg/mL. UseTBS with 3% nonfat milk asthe diluent.Secondary antibody cross-reactivity.For the secondary antibody, it isrecommended that users initiallyemploy dilutions of 1:30,000.Higher dilutions may be necessary,or a more specific secondaryantibody should be used.Monoclonal ANTI-FLAG® M2antibody cross-reacts with naturallyoccurring FLAG®-like epitopes.Increasing the temperature to37 °C during the blocking, binding,and wash steps may reducecross-reactivity. Lysates frommock-transfected controls(transfected with plasmid lackinginsert DNA) will help distinguish theFLAG®-fusion proteins from othercross-reacting proteins.NoticeWe provide information and advice to our customers on application technologies and regulatory matters to the best of our knowledge and ability, but without obligation or liability. Existing laws and regulations are to be observed in all cases by our customers. This also applies in respect to any rights of third parties. Our information and advice do not relieve our customers of their own responsibility for checking the suitability of our products for the envisaged purpose.The information in this document is subject to change without notice and should not be construed as a commitment by the manufacturing or selling entity, or an affiliate. We assume no responsibility for any errors that may appear in this document.Technical AssistanceVisit the tech service page at /techservice.Standard WarrantyThe applicable warranty for the products listed in this publication may be found at /terms. Contact InformationFor the location of the office nearest you, go to /offices.。

美国食品与药品管理局批准一种新甜味剂
佚名
【期刊名称】《现代化工》
【年(卷),期】2003(23)6
【总页数】1页(P67-67)
【关键词】美国食品与药品管理局;批准;甜味剂neotame;美国NutraSweet公司;甜度
【正文语种】中文
【中图分类】TS264.9
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5.2007—2009年美国食品药品管理局批准的新抗微生物药物和已批准药物的新适应证 [J], 袁瑾懿;王明贵
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专利名称：一类具有抗炎活性的熊果酸噁唑啉类新药及其制备方法
专利类型：发明专利
发明人：杨定菊,蒋睿,邓聪,石万棋,支春,李颖
申请号：CN200710050797.6
申请日：20071214
公开号：CN101182345A
公开日：
20080521
专利内容由知识产权出版社提供
摘要：本发明公开了具有抗炎的熊果酸类衍生物及其制备方法。

该类化合物具有良好的抗炎作用。

该类熊果酸类衍生物新药具有如下化学式(I)。

本发明所提供的熊果酸类衍生物是具有抗炎活性，它以熊果酸为母体化合物，根据药物构效分子学的原理进行结构修饰，设计并制备了治疗炎症功能的具有高活性的化合物。

申请人：四川国康药业有限公司
地址：610091 四川省成都市青羊区文家场蛟龙工业港高新区A区18座
国籍：CN
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专利名称：ANTIBIOTIC A-25822发明人：ROBERT HOWARD WILLIAMS,MARVIN MARTIN HOEHN,KARL HEINZ MICHEL 申请号：AU5232273申请日：19730219公开号：AU5232273A公开日：19740822专利内容由知识产权出版社提供摘要：1369179 Aza-steroidal antibiotics A-25822 ELI LILLY & CO 16 Feb 1973 [29 Feb 1972 2 Feb 1973] 7805/73 Heading C2A Novel antibiotic substances having an azasteroid structure and designated generally as A-25822 antibiotics are produced by cultivating Geatrichium flavo-brunneum NRRL 3862 under submerged aerated conditions in an aqueous nutrient medium containing assimilable sources of carbon, nitrogen and inorganic salts until a substantial amount of antibiotic activity is present in said medium, and then recovering the said antibiotics therefrom. The individual antibiotic compounds, factors A, B, D, H, L, M and N are then isolated from the resulting mixture, or alternatively separately isolated from the fermented broth. A-25822-A, B and M have the general Formula (I) wherein for factor A, R 1 and R 2 are each methy and R 3 is hydroxy; for factor B, R 1 and R 2 are each hydrogen and R 3 is acetoxy; and for factor M, R 1 and R 2 are each hydrogen and R 3 is hydroxy. Factor N has the formula Accordingly using the homosteroidal nomenclature system in which " 14a " is used to designate the ring enlarging atom, factor A is 3# - hydroxy - 24 - methylene - 14a - aza - D- homo - 4,4 -dimethyl - 5 - α - cholest - 8(9),14- (14a) - diene; Factor B is 3# - hydroxy - 24- methylene -14a - aza - D - homo - 5α - cholest - 8- (9),14(14a)-diene; and factor M (the acetate offactor B) is 3#-acetoxy-24-methylene-14a-aza-D- homo - 5α - cholest - 8(9),14(14a) -diene. Factor N is 24-methylene-14a-aza-D-homo-5α-cholest-8- (9),14(14a)-dien-3-one. The factors D, L and H are mainly characterized and defined by their physico-chemical characteristics since their structures have not definitely been determined. However factor D is preferably a 15-hydroxy substituted factor B, namely 3,15-dihydroxy-24-methylene-14a-aza- D - homo - 5α - cholest - 8(9),14(14a) - diene, and factor L is probably a 15-keto derivative of factor B, namely 3#-hydroxy-24-methylene-14aaza - D - homo - 5α - cholest - 8(9),14(14a) - diene- 15-one. Factor D is a white amorphous compound, melting at 51-55‹ C., having amolecular weight of 427 and an empirical formula: C 28 H 45 NO 2 , a specific rotation [α]25 D = +39 degrees (C = 0À725 MeOH), a U.V. absorption maximum, #max at 235 mÁ in EtOH and at 270 mÁ in acid. Factor L is a yellowish amorphous compound having a molecular weight of 425 and an empirical formula: C 28 H 43 NO 2 , a specific rotation [α]25 D = +75 degrees (C = 0À072, MeOH), a U.V. absorption maximum, #max at 262 mÁ in basic and neutral solution and at 279 mÁ in acid. Factor H is a white amorphous compound melting at 74-77‹ C., having a molecular weight of 425 and an empirical formula: C 28 H 43 NO 2 , a specific rotation [α]25 D = +15 degrees (C = 0À147, MeOH), a U.V. absorption maximum, #max at 235 mÁ in basic and neutral solution and at 270 mÁ in acid. The compounds containing hydroxyl groups can be converted to their acetate esters by treatment with acetic anhydride in pyridine. For example factors A, B and L form mono-acetyl derivatives, and factor D forms a diacetyl derivative; factor B monoacetate is identical with factor M (i.e. R 1 = R 2 = H, R 3 = acetoxy, in the above Formula I). All of the compounds form acid-addition salts with organic and inorganic salts and react with methyl iodide to form crystalline methiodide salts. Factor B as the free base exhibits polymorphism (probably due to different diastereoisomeric forms) when crystallized from different solvents; e.g. melting points of 56-58‹ C., 42-44‹ C. and 115-118‹ C., with differing X-ray diffraction patterns, when crystallized from n-hexane, pentane and an acetone-hexane mixture respectively. The antibiotics are recovered from the culture broth, mainly from the mycelium, by extraction with an organic solvent (e.g. ethylacetate), purified by conventional washing and backextraction procedures, and the individual components are then separated by column chromatography and fractional crystallization. They may be used with a suitable carrier or diluent in antibiotically active pharmaceutical compositions and in disinfectant compositions.申请人：LILLY, ELI & CO.更多信息请下载全文后查看。

小学上册英语第一单元测验试卷英语试题一、综合题(本题有100小题，每小题1分，共100分.每小题不选、错误，均不给分)1.My mom makes the best ______ (soup).2.What is the name of the ocean that is the largest?A. AtlanticB. IndianC. ArcticD. Pacific3.What is the name of the largest mammal on Earth?A. ElephantB. Blue WhaleC. GiraffeD. Hippopotamus4.The chemical formula for sodium selenate is __________.5.The pencil is ________ on the desk.6.The __________ is a region known for its history.7.What is the main ingredient in chocolate?A. CocoaB. WheatC. RiceD. Sugar8.Seeds can be stored for __________ (未来使用).9.What is the term for a young tortoise?A. HatchlingB. CalfC. PupD. KitA10.can Civil Rights Movement took place in the ________ (1960年代). The Amer11.What do you call the process of making cheese?A. FermentationB. PasteurizationC. CurdlingD. CreamingC12.What is the sound of a cow?A. BaaB. MooC. QuackD. Roar13.What is the name of the famous American author known for his short stories?A. Edgar Allan PoeB. Nathaniel HawthorneC. F. Scott FitzgeraldD. All of the aboveD14.We have a ________ (花园) in our backyard.15.What is the name of the large flightless bird native to Australia?A. PenguinB. OstrichC. EmuD. KiwiC16.My best friend is very ________ and kind.17. A molecule is made up of two or more ______ bonded together.18. A mixture that appears uniform but contains particles is called a _______ mixture.19.I like to ___ (listen/sing) to songs.20.I saw a ________ crawling on the ground.21.The dog is ___ at the park. (running)22.How many years are in a century?A. 50B. 100C. 150D. 200答案:B23.The chemical formula for -octanoic acid is ______.24.What do you call the king of the jungle?A. TigerB. ElephantC. LionD. Bear25.My sister loves to play with ______ (小猫).26.What do we call the large body of freshwater that is smaller than an ocean?A. RiverB. SeaC. LakeD. PondC27.Fossils are often found in sedimentary ______ that formed over millions of years.28.The ant is very ________________ (勤劳).29.My ______ is very supportive and caring.30.My sister enjoys __________ (参加) workshops.31.What is the name of the famous American holiday celebrated on July 4th?A. ThanksgivingB. Independence DayC. Labor DayD. Memorial DayB32.Salt can be formed by the reaction of an acid and a _____ (base).33.My favorite animal is a ______ (老虎).34.The capital city of Belgium is ________ (比利时的首都城市是________).35. A rabbit can hop very ________________ (快).36. A ________ is a landform that is higher than the land around it.37.What is the color of a typical cat?A. BlackB. WhiteC. GrayD. All of the above38.What is the name of the first spacecraft to capture images of the far side of the moon?A. Apollo 11B. Luna 3C. Voyager 1D. Mariner 1039.I put my _______ (shoes) by the door.40.Every morning, I eat ________ (早餐) before school.41.What is the color of an orange?A. YellowB. OrangeC. PurpleD. BlueB42.I built a tower with my ____. (积木)43.The ______ (花瓣的排列) can attract specific pollinators.44.She is learning to ________.45.The capital of Fiji is ________ (苏瓦).46.The ________ loves to play with its toys.47.Vines can _____ (攀爬) up walls and fences.48.My grandma loves her _______ (我奶奶爱她的_______).49. A walrus can weigh over a ________________ (吨).50.Chinchillas have very soft _________. (毛)51.The owl's exceptional hearing allows it to hunt effectively in ________________ (黑暗).52.Which of these is an insect?A. SpiderB. AntC. SnailD. Worm53. A bunny's feet are very ______ (强壮).54.What is the name of the fairy tale character who climbed a tower?A. CinderellaB. RapunzelC. Snow WhiteD. Little Red Riding HoodB55.The __________ were a group of explorers who circumnavigated the globe. (麦哲伦的探险队)56.I think teamwork is essential. In group projects, I like to __________.57.I like to play ________ (橄榄球) with my friends at school.58.Planting trees can help reduce ______ (污染).59.Which month is the start of the year?A. FebruaryB. MarchC. JanuaryD. DecemberC60.The fireflies are ______ (glowing) at night.61.We are going to ________ a picnic.62.My favorite color is _____ (蓝色).63.How many sides does a hexagon have?A. FourB. FiveC. SixD. SevenC64.What is the color of the sky during a sunset?A. BlueB. RedC. GreenD. Yellow65.The clock shows ______ (three) o'clock.66.What is the capital city of Australia?A. SydneyB. MelbourneC. CanberraD. Brisbane67.green architecture) promotes sustainable building practices. The ____68.What is the main purpose of a playground?A. To exerciseB. To relaxC. To playD. To socializeC69.My favorite pet is a _______ (狗).70.I enjoy ______ (制作) crafts for my family.71.The ice cream is ______ on a hot day. (refreshing)72.The chemical formula for iron(III) oxide is __________.73.Martin Luther King Jr. delivered his famous "I Have a Dream" speech in ______ (1963年).74.My ______ loves to study languages.75.My friend has a lovely _______ (动物). 它的性格很 _______ (形容词).76.Which fruit is red and often used in pies?A. BananaB. CherryC. GrapeD. OrangeB77.I enjoy _______ (参加) cultural festivals.78.My favorite subject is ______ (history).79.The teacher gives us ______ for being good. (stickers)80.My _____ (女儿) loves to plant flowers in the spring. 我女儿喜欢在春天种花。

2018年4月20日第27卷第8期v〇i. 2.7, n〇. 8, A p ril 2〇,2018______________________China Pharmaceuticals.硏究. Drug Research•实验研究•d o i: 10. 3969/j.issn. 1006 -4931. 2018. 08. 001姜黄素脂质体载药量与体外抗瘤效果的关系+王雪婷，李宁，刘婷，蒋少鸿，邱昌露，王汀△(安徽医科大学药学院，安徽合肥230032)摘要：目的探讨不同载药量的姜黄素纳米脂质体（简称CUR -N L)对不同肿瘤细胞的抑制效果。

方法采用薄膜分散法制备C U R-N L，以低速离心法测定包封率。

噻唑蓝（M T T)法检测不同载药量的C U R-N L对H e p G2细胞、SG C-7901细胞、B e l-7402细胞的抑制作用。

结果CUR - N L(0. 5 mg)与CUR - N L(0. 25 m g)的包封率分别为（87. 06 ± 2. 37)%和（95. 27 ± 2. 60)%;C U R - N L 对上述 3 种肿瘤细胞均有抑制作用，抑制作用呈时间-剂量依赖性；当给药总剂量相同时，载药量与抗瘤效果并不呈正相关。

结论对于HepG2,SGC -7901，B e-7402肿瘤细胞而言，提高姜黄素载药量并不能提高抗瘤活性。

关键词：药剂学；纳米脂质体;姜黄素；载药量；抗瘤活性中图分类号：R285.5;R273文献标识码：A文章编号：1006-4931牗018) 08 -0001-05Relationship Bet^veen Drug Loading Capacity and in Vitro A ntitumor Effect of CurcuNanoliposomesng Xueting，Li N i n g,Liu T ing，Jiang Shaohong，Qiu Changlu , Wang(School of Pharmacy , Anhui Medical U n,A b s tra c t ： O bjective To investigate the relationship between the inhibitory efects on tumor cells and drug loading capacity of curcuminnanoliposomes(CUR - N L). M ethods CUR - NL was prepared by thin - film dispersion method and the entrapment efficiency was mea­sured by low -speed centrifugation. The inhibitory effects of C U R-N L on HepG2 cells , S G C-7901cells and Bel - 7402 cells wereexplored by MTT assay. Results The entrapment rates of CUR - N L(0. 5 mg) and CUR - N L(0. 25 mg) were (87. 06 ±2. 37)%and(95．27 ± 2. 60)%, respectively. CUR - N L had higher inhibitory effect on the three tumor cells in the time and dose - dependent manner.When the total dose was id e n tica l, CUR -NL w ith different curcumin loading capacities did not show a difference in the antitumoreffect. C onclusion Enhancement of drug loading capacity of curcumin can't enhance antitumor effects on H epG2, SGC - 7901and Bel - 7402 tumor cells.K e y w o rd s: pharmaceutics; nanomaterials; curcum in; drug loading; antitumor activity姜黄素（curcumin,Cur)是从姜黄根茎提取出的结晶性黄色多酚类物质[1]，具有抗毒、抗氧化[2]、抗糖尿病 肾病[3]、降血糖[4]和防治血栓形成[5]等作用，尤其是具有 较强的抗肿瘤活性犤-7犦且不良反应少，药源充足，具有 较好的开发前景[8]。

flavors 用法-回复Flavors are an essential component of our daily lives. From the food we eat to the scents we enjoy, flavors play a vital role in creating memorable experiences. In this article, we will delve into the various aspects of flavors, exploring their origins, applications, and impact on our senses.To begin with, let's understand the concept of flavors. Flavors can be described as the taste or odor of a substance, resulting from the combination of various chemical compounds. These compounds interact with our taste buds and olfactory receptors, creating a unique sensory experience.The origins of flavors can be traced back to nature. Many flavors are derived from plants, fruits, spices, and other natural sources. For example, the refreshing taste of mint, the zingy flavor of citrus fruits, and the warm aroma of cinnamon all come from natural sources. These flavors are extracted through various methods such as distillation, cold-pressing, and solvent extraction.In addition to natural flavors, there are also artificial flavors. Artificial flavors are synthesized in a laboratory to mimic the tasteor aroma of natural substances. While some may argue that artificial flavors lack the complexity and depth of natural flavors, they have their own merits. Artificial flavors allow for consistency in taste and are often used to enhance or modify existing flavors. They are widely used in the food and beverage industry to create a wide range of products.Flavors have countless applications, with the food industry being one of the primary users. The incorporation of flavors can transform a bland dish into something extraordinary. From sauces and seasonings to desserts and beverages, flavors are used to enhance the taste and appeal of food products. They can evoke nostalgia, create comfort, or provide a unique sensory experience.Flavors are not limited to just food and beverages. They are also extensively used in the cosmetic and personal care industry. Fragrances, perfumes, and scented products rely heavily on flavors to create a pleasant smell. Flavors can transport us to different places, evoke emotions, and even enhance our mood. Whether it's the soothing scent of lavender in a body lotion or the invigorating aroma of citrus in a shampoo, flavors play a crucial role in creating a luxurious and enjoyable experience.Furthermore, flavors can also have a significant impact on our emotions and memories. Have you ever experienced a sudden rush of memories when smelling a familiar scent or tasting a specific flavor? This phenomenon is known as aroma-evoked nostalgia. Flavors can trigger powerful memories, taking us back to a specific time or place. This connection between flavors and memories is deeply rooted in our brain, as our olfactory system is closely linked to our limbic system, which is responsible for emotions and memory.The study of flavors, known as flavor science, is a multidisciplinary field that combines chemistry, biology, psychology, and sensory evaluation. Scientists in this field explore the chemical composition of flavors, their interaction with taste receptors, and the perception of flavors by our senses. This knowledge is used to develop new flavors, improve existing ones, and even create healthier alternatives by reducing sugar, salt, or fat content without compromising on taste.In conclusion, flavors play a crucial role in our daily lives. From the foods we eat to the scents we enjoy, flavors enhance our sensoryexperiences, evoke emotions, and create lasting memories. Whether natural or artificial, flavors have countless applications in the food, cosmetic, and personal care industries. The study of flavors continues to evolve, with scientists constantly striving to unlock the mysteries of taste and aroma. So the next time you savor a delicious meal or appreciate a delightful fragrance, take a moment to appreciate the power and beauty of flavors.。