浅析钩针编织在现代纤维艺术中的应用——以《纯白之漪》系列作品为例

钩针编织普及化的时间大约在 19 世纪的欧洲, 通过一些文字资料的记载,最早的钩针编织是通过手指完 成的,而不借助于钩针工具。虽然具体的钩针编织历史无 法追溯,但是钩针编织在近现代艺术中散发了熠熠生辉的 光芒。纤维艺术是一门复杂的交叉性学科,也是一种既古 老又年轻的艺术形式。纤维艺术起源于壁毯艺术,高比林 壁毯以其卓越的工艺和精细的编织而闻名于欧洲,壁毯艺 术的发展也推动了纤维艺术的发展。本篇文章通过《纯白 之漪》系列作品,研究钩针编织在现代纤维艺术中的应用。

《纯白增上心问难》一文是否为宗喀巴大师所作辨析

关于藏文文献《纯白增上心问难》是否为宗喀巴大师所作,学界众说纷纭,各抒己见,成为争执不休的焦点之一。虽然过去多数藏族学者对其持肯定的态度,但也有不少持怀疑态度的学者,如宗喀巴大师的亲传弟子班禅强巴林巴、土观·洛桑曲吉尼玛等等。他们对此提出的一系列质疑,曾一度成为学界所关注的热点。文章在借鉴前人研究成果的基础上,运用比较研究方法,专门对该文献是否宗喀巴所作进行了学理探究。从文辞、文风、文法特点以及资料引用路径等方面的比较研究,认为《纯白增上心问难》一文确系宗喀巴大师所作。

纯白守护 一定会相见

“小迪，我昨天梦见雪人了!”迪音靠在树荫下休息，静恋儿气喘吁吁地跑过来，“他竟然让我忘记他。”

纯白守护之真相大白

终于下雪了，彗花在天空中飘着、把蓝天点缀得格外可爱。 “雪花真美啊!”静恋儿透过玻璃望着窗外感叹道。几乎每次下雪的时候她都要这么说。

纯白守护弥月驾到

清晨，和煦的阳光倾洒在街道两旁，迪音收拾好书包准备出门去学校。在雪山中虽然自动魔力保护了静恋儿，但她还是受了一些轻伤，在医院里静养了好一段日子。今天是她出院的时候，想必今天，她也会去上学吧。

Purification and Immunocompetence Analysis of GP5 Protein in Porcine Reproductive and Respiratory Syndrome

[Objective] The purification and immunocompetence of GPS protein in porcine reproductive and respiratory syndrome (PRRS) were analyzed in this study, which provided basis for establishing the corresponding serological method. [Method] The recombinant expression plasmid pGEX-6P-5 was transformed into BL21 and expressed after being induced with IPTG. The solubility analysis of expression products was carried out, and then the recombinant protein was purified for SDS-PAGE identification and Western-blot analysis. Finally, the recombinant antigen was used in the immune experiment of guinea pigs. [Result] The target protein content accounted for 30% of the total cells protein content according to the chromatography scanning, and the purity of target protein after purification reached 80%. The purified protein was analyzed by Western-blot and immune experiment of guinea pigs, and the results showed that the expressed protein had good reactionogenicity and immunogenicity. [Conclusion] This study provides materials for further studies on the function between PRRSV ORF5 gene and its editing protein, which also lays a foundation for porcine reproductive and respiratory syndrome virus genetic engineering products.

Expression,Purification and Activity Detection of VP1 of A-type FMDV

[Objective] The research aimed to induce the expression of FMDV structural protein VP1 in E.coli and purify the protein,then detect the activity.[Method] The fragment coding VP1 was amplified by PCR and doubly digested with BamH Ⅰ and XhoⅠ,then cloned into expression vector pGEX-4T-1 and pPROExHTb respectively to get recombinant plasmid pGEX-4T-1-VP1 and pPROExHTb-VP1.The recombinant plasmid pGEX-4T-1-VP1 and pPROExHTb-VP1 was transformed into E.coli BL21(DE3)and induced by IPTG,fusion protein was identifie...

Large_scale Isolation and Purification of R_phycoerythrin from Red Alga Palmaria palmata Using the Expanded Bed Adsorption Method

R-phycoerythrin, a light-harvesting protein in some marine algae, and can be widely used in medicine, was isolated and purified from a red alga, Palmaria palmata (Lannaeus) Kuntze, using the streamline column (expanded bed adsorption) combined with ion-exchange chromatography. Because the crude extract was applied to the column upwardly, the column would not be blocked by polysaccharides usually very abundant in the extract of marine alga, this kind of blockage could hardly lie overcome in ordinary chromatographic column. After applying the crude extract containing 0.5 mol/L (NH4)(2)SO4, (NH4)(2)SO4 solution of different concentrations (0.2 mol/L, 0.1 mol/L and 0.05 mol/L) was used to elute the column downwardly and the eluates were collected and desalted. The desalted eluates were then applied onto all ion-exchange chromatographic column loaded with Q-sepharose for further purification of the R-phycoerythrin. Through these two steps, the purity (OD565/OD280) of the R-phycoerythrin from P. palmata was up to 3.5, more than 3.2, the commonly accepted criterion for purity, and the yield of the purified R-phycoerythrin could reach 0.122 mg/g of frozen P. palmata, much higher than that of phycobiliproteins purified with the previous methods. The result indicated that the cost of R-phycoerythrin will drop down with the method reported in this article.

Purification and Antimicrobial Activity of Antimicrobial Protein from Brown-spotted Grouper, Epinephelus fario

Antimicrobial proteins and peptides had been found from a wide variety of organisms in the last few years These molecules have attracted much research interest because of their biochemical diversity, broad specificity on anti-viral, anti-bacterial, anti-fungi, anti-protozoan parasites, anti-tumoural, and wound-healing effects. Antimicrobial proteins and peptides play key roles in innate immunity. They interact directly with bacteria and kill them. The brown-spotted grouper, Epinephelusfario, is an important marine fish cultured in southem China. Recently, bacteria and virus have caused high mortality in E. fario cultures, but its endogenous antimicrobial peptides and proteins have not been explored. An antimicrobial component was found from the skin homogenate of E. fario. After the skin homogenate was digested with trypsin, its antimicrobial activity was lost, which showed that the antimicrobial component is a protein. The antimicrobial protein （Efap） was purified from the skin homogenate of E. fario by successive ion-exchange and gel filtration chromatography. Efap was demonstrated to be single protein band by SDS-PAGE, with the apparent molecular weight of 41 kD. Efap exhibited antimicrobial activity both for the Gram-positive bacteria, Staphylococcus aureus, Micrococcus luteus and Bacillus subtilis, and for the Gram-negative bacteria, Vibrio alginolyticus, Vibrio parahaemolyticus, Vibrio fluvialis, Pasteurella multocida, Aeromonas hydrophila, Eschrrichiu coli, and Pseudomonas aeruginosa. Except A. hydrophila, P. aeruginosa, and E. coli （MIC〉20 mol/L）, most of the tested Gram-negative bacteria were sensitive to Efap （MIC〈20 mol/L）. Interestingly, Efap showed potent antimicrobial activity against Gram-positive bacteria S. aureus （MIC 5-10 mol/L） but comparatively weak antimicrobial activity against M. luteus and B. subtilis. The broad antimicrobial activities of Efap suggest that it contributes to the innate host defence of E. fario.

Purification and Antimicrobial Assay of an Antimicrobial Protein from a Biocontrol Bacterium Strain K2-1 against Aquatic Pathogens

[Objective] The aim of this study was to purify an antimicrobial protein from a biocontrol bacterium strain K2-1 and analyze its antimicrobial activity in vitro against some typical aquatic pathogens. [Method] The antimicrobial protein was ob- tained by using ammonium sulfate precipitation and Sephadex chromatography combined with hot water bath. The antimicrobial assay was conducted by means of agar diffusion technique, using Vibrio alginolyticus, Aeromonas hydrophila, Aeromonas. Sobria, Pseudomonas fluorescens, Vibrio Parahaemolyticus, Vibrio har- veyi and Vibrio anguillarum as test bacteria. [Result] Antimicrobial protein APK2 can be derived from fermentation broth of strain K2-1 and purified to the chromatogra- phy pure level by the methods provided, the final yield of the antimicrobial compo- nent is approximately 0.08%. This antimicrobial protein had a strong antimicrobial activity against the growth of most those bacteria. [Conclusion] The results show that APK2 could be a potential alternative to replace chemical antimicrobial agent in the control and prevention of aquatic diseases.

Purification and Characteristics of Mn-containing Nitrogenase Component Ⅰ

A mutant UW 3, which is unable to fix N 2 in the presence of Mo (Nif -) but undergo phenotypic reversal to Nif + under Mo deficiency, was able to grow in Mo- and NH 3-deficient medium containing Mn, and the growth was accelerated by Mn at low concentration. A partly purified nitrogenase component Ⅰ protein separated from UW 3 grown in the Mn-containing medium was shown to contain Fe and Mn atoms (ratio of Fe/Mo/Mn: 10.41/0.19/1.00) with C 2H 2- and H +-reducing activity which almost equal to half of that of MoFe protein purified from wild-type mutant of Azotobacter vinelandii Lipmann. This protein was obviously different from MoFe protein in both absorption spectrum and circular dichroism, and the molecular weight of subunits in Mn-containing protein was close to that of α subunit in MoFe protein. The preliminary results indicated that the protein containing Mn might be a nitrogenase component Ⅰ protein.

Affinity Chromatography Purification of Recombinant Human Interleukin-6 from Its Fusion Protein with GST

Recombinant E.coli JM109, containing pHZ1818 plasmid which included the fused gene encoding human interleukin 6(IL 6), expressed a fusion protein with glutathion S transferase(GST). The fusion protein existed both in the supernatant and inside the bacterial cell,but the insoluble protein had no biological activity and could not be refolded. The rotative speed of the shaker and the temperature of induction were optimized to maximize the expression of the soluble fusion protein. From the supernatant of the cell sonicates Glutathion Sephrose 4B affinity column chromatography was employed to isolate the fusion protein which could be purified to >80 0 0 in a single step. The yield of soluble GST IL 6 was about 10 mg per liter culture. The GST was site specifically cloven by 6 hours of treatment with thrombin and from the thrombin digest mixture IL 6 was purified by Q high performance ion exchange chromatography. From 1 liter of E.coli culture 2 mg refined IL 6 was obtained. The purified IL 6 had a purity of more than 95 0 0 and a biological activity of 1.02×10 8 IU/mg.

Establishment of an Indirect ELISA with the Major Epitope Domain of ApxⅡ of Actinobacillus pleuropneumoniae Expressed in Prokaryotic Cells

[Objective] This study aimed to develop an indirect ELISA to detect the antibodies against Actinobacil us pleuropneumoniae （APP） using the recombinant ApxⅡA1 protein expressed in prokaryotic cells as the antigen. [Method] The major epi-tope domain of ApxⅡ was cloned into the prokaryotic expression vector pET-28a （＋） to obtain the recombinant plasmid pET-ApxⅡA1, which was then transformed into E. coli BL21 （DE3） for expression. The immunogenicity of the recombinant pro-tein was analyzed by western-blotting. After that, the purified recombinant protein was used as the coating antigen in the indirect ELISA for detecting the antibodies against APP. Final y, the concentration of coated antigen and the dilution of serum were optimized. [Result] Proved by enzyme digestion and sequencing, the recombi-nant plasmid pET-ApxⅡA1 was constructed successful y. The recombinant protein was highly expressed in prokaryotic cells, and Western-blotting analysis showed that it was recognized specifical y by positive serum of APP. The indirect ELISA could detect the antibody against APP with the purified recombinant protein as the coating antigen. The optimal concentration of coated antigen was 1.23 μg/ml and the opti-mal dilution of serum was 1：100. Compared with a commercial ELISA kit detecting antibody against ApxⅣ, the coincidence rate of the indirect ELISA was 90.4%. [Conclusion] Our results indicated that the indirect ELISA is sensitive and specific, and suitable for evaluating the effect of APP vaccine and epidemiological surveys.

纯白

被白昼惊醒。散乱的梦还恍惚着，无法拼凑成节，像上一季云烟似的过往。我翻过身，翻过暗夜里那些荒唐恐怖的片段。光斜斜地照进来，越过厚厚的窗幔和一些游离的物质，亲近我。眼前是烫手的七月，它光芒得多么纯白。

Purification and Characterization of a Cathepsin B-Like Proteinase from Eggs of Antheraea Pernyi

A cathepsin B-like proteinase was purified from eggs of Antheraea pernyi by 5 steps of purification. The molecular mass of the proteinase are estimated to be 47 kDa by using SDS-polyacrylamide gel electro-phoresis. The activity of the purified proteinase were strongly inhibited by E-64 and Leupeptin. The optimum pH is 3.5 as determined by using the bovine hemo-globin as substrate. The activity and quantity of the proteinase during embryo development were studied. The results suggested that the proteolytic activities during embryo development at least partially came from this proteinase.

Extraction, Purification and Identification of Bone Morphogenetic Protein in Conditioned Medium of Osteosarcoma Cell (MG-63)

Objective: To find out a method of extraction and purification of bone morphogenetic protein (BMP) from osteosarcoma cell conditioned medium, and evaluate the biological activity of BMP.Methods: Conditioned medium of osteosarcoma cell lines (MG-63) was collected, concentrated and dialyzed. The concentrated protein was purified through gel chromatography on Sephcryl-S-100. The purified protein was tested by BMP monoclonal antibody (McAb), its molecular weight (MW) was determined by SDS-PAGE and its biological activity was demonstrated by heterotopic ossification.Results: The purified protein was proved to be BMP by BMP McAb, had a satisfactory heterotopic ossification, and its MW was about 21 kD.Conclusion: BMP existed in the conditioned medium of osteosarcoma cell and had a satisfactory biological activity after purification. Because osteosarcoma cell can be cultured and grew for a long timein vitro, this method will be helpful to a vast extraction of BMP and clinical application. Key words osteosarcoma cell - conditioned medium - bone morphogenetic protein - protein purification This project was a key scientific and technological program of Hubei Provicial Scientific and Technological Committee (No. 002p1503).

Signal-purity-spectrum-based colored deconvolution

Signal to noise ratio （SNR） and resolution are two important but contradictory characteristics used to evaluate the quality of seismic data. For relatively preserving SNR while enhancing resolution, the signal purity spectrum is introduced, estimated, and used to define the desired output amplitude spectrum after deconvolution. Since a real reflectivity series is blue rather than white, the effects of white reflectivity hypothesis on wavelets are experimentally analyzed and color compensation is applied after spectrum whitening. Experiments on real seismic data indicate that the cascade of the two processing stages can improve the ability of seismic data to delineate the geological details.

纯白

家中书房的书架上，放着一卷中国画。我有时会拿出来看看，看完后，脸上总会挂着舒畅的笑容。姨婆是丹青好手。她早年开始画国画，一开始是为了消磨时间，后来便一发不可收拾。

Purification and Characterization of Cr-containing Nitrogenase Component Ⅰ

A mutant UW 3, which is unable to fix N 2 in the presence of Mo (Nif -) but can undergo phenotypic reversal to Nif + under Mo_deficient conditions, was able to grow in Cr_containing but Mo_ and NH 3_deficient medium. A partly purified nitrogenase component Ⅰ protein obtained from UW 3 grown on the Cr_containing medium was shown to contain Fe and Cr (atom ratio of Fe to Cr and Mo to Cr: 11.60 and 0.41) and to have 70% of the C 2H 2_ and H +_reduction activity of MoFe protein from the wild_type strain of Azotobacter vinelandii Lipmann. The Cr_containing protein was different in subunit composition from that of MnFe protein purified from the mutant strain grown in the presence of Mn, but similar to that of MoFe protein, that is, it was a tetramer composed of two different subunits (α 2β 2). The preliminary results indicated that the Cr_containing protein might be a nitrogenase component Ⅰ protein.

Purification and Characterization of Flammulin,a Basic Protein with Anti-tumor Activities from Flammulina velutipes

Aim To purify and characterize flammulin, a basic protein with anti-tumoractivities. Methods Ammonium sulfate, ethanol fractionation and column chromatography were used forseparation and purification. Electrophoretic analysis, amino acid analysis, and MS of flammulin werecarried out. Results Flammulin was purified to electrophoretic homogeneity and crystallized. With amolecular mass of 19891.13 Da, pI 8.9, λ_(max) = 276 - 278 nm, λ_(min) = 250 nm, flammulin wascharacterized by its lack of methionine. Fingerprint mapping of flammulin was determined by MALDI-MSfollowing in-gel protease digestion; no close matches were identified. Conclusion Flammulin waspurified to electrophoretic homogeneity, and its characteristics are discussed for the first time.