虎杖染料超声辅助蚕丝织物染色工艺

为有效降低染色能耗与排放,本文从植物虎杖中提取了天然染液染色蚕丝织物,并研究了超声辅助染色相较于传统染色技术的优势.确定了染色蚕丝织物最佳工艺条件:预处理最佳条件为8 g/L的碳酸钠溶液,超声处理20min,浴比1∶8;染色最佳工艺为:染液浓度:80％;染色温度:60℃;染色时间35 min.     

黄芩苷对聚酯PET纤维的染色

采用天然染料黄芩苷对聚酯PET纤维进行染色,研究了黄芩苷染色pH值、温度、时间、黄芩苷用量对PET纤维表观色深的影响,探讨了黄芩苷在PET纤维上的升温上染速率曲线以及染色织物的牢度.研究表明,当染色温度在120～130℃之间、pH值为5左右时,黄芩苷对PET纤维具有较好的上染性能;在一定的染料用量范围内,黄芩苷在PET...     

大豆/PTT微胶囊分散染料/活性染料一浴一步法染色

探讨了纯碱和氯化钠用量、染料浓度对微胶囊分散蓝2BLN/活性染料(活性蓝KN-R、活性深蓝B-2GLN和活性蓝K-3RL)一浴法染色大豆/PTT混纺织物表观色深K/S值的影响,测定了不同染色工艺对染色织物牢度的影响.结果表明:当染料总用量为2％(o.w.f.),纯碱用量1g/L,氯化钠用量20 g/L,95℃条件下保温30分钟时,可使大豆/PTT混纺织物获得较高的表观色深.     

碱性染料在蔺草染色中上染率和摩擦牢度的研究

选用碱性兰染料对蔺草进行染色,探讨染液pH值、染色保温温度、染料用量、电解质的用量及染色保温时间对蔺草上染率和摩擦牢度的影响,结果表明,用碱性兰染料对蔺草进行染色时,最佳上染率和摩擦牢度的工艺条件是:染液pH值7～10,染色保温温度80℃,染色温度在70℃以下时升温速率控制在3℃/min,染色温度在70～80℃时升温速率控制在1℃/2 min,染料用量为0.5%～1%(owf),元明粉用量10 g/L,染色保温时间20 min。     

染色废水的还原脱色及其回用

使用还原型双组分脱色剂对含有不同种类水溶性染料的染色废水进行脱色处理，重点研究了脱色剂用量、反应温度、pH值和时间对脱色反应的影响。并且将脱色后的染色废水回用于织物染色中，在染料的上染速率曲线和颜色特征方面进行了比较。结果表明，随着脱色刑用量的增加，染色废水的脱色率都逐渐升高：中性pH条件和温度的升高均可以促进染色废水的脱色；在60℃～700℃，脱色率可达到90％；在常温下3～5分钟内完成脱色，而直接染料不超过15分钟，脱色废水能够回用于织物染色中，染料的上染曲线几乎没有变化，染色深度和色差变化极小。     

西藏本土天然植物蕞提取液对氆氇染色工艺的研究

采用超声波提取法对西藏本地植物蕞进行提取,而后用提取液对氆氇进行媒染染色,探讨了染料提取方法、提取工艺、染色工艺、媒染剂种类、媒染剂用量、提取液用量、染液pH、染色温度和时间对氆氇染色性能的影响,并测试了染色氆氇的染色牢度。结果表明：采用超声波提取法提取染液,染色工艺为前媒染色法;染料用量50m L/L,硫酸亚铁（0.5g/L）,染色时间为120min,染浴的p H值为5,染色温度为85℃。此时,染色氆氇的耐水洗色牢度可达3～4级,耐摩擦色牢度可达4级及以上。     

纯棉织物涂料染色工艺的研究

本文研究了阳离子改性纯棉针织物荧光涂料染色的新工艺,系统分析了涂料浓度、染色温度、粘合剂用量、焙烘温度等工艺参数对涂料染色织物各项性能的影响。通过测定染色织物的K/S值、摩擦牢度、皂洗牢度,得到柠檬黄荧光涂料对阳离子改性纯棉针织物染色的最佳工艺配方:涂料浓度为0.5%~3%(o.w.f.),染色温度为60℃,粘合剂用量为5 g/L,焙烘温度为120℃。     

对位芳纶染色工艺研究

研究了载体助剂、染色温度、染色保温时间、pH值、缓染剂染色因素对对位芳纶染色效果的影响.结果表明:载体用量30g/L,染色温度140℃,染色保温时间60 min,pH值为3～4为最佳工艺条件.选择氯化钠作为缓染剂对织物染色后色深值影响较小.     

涤/棉复合裂片型超细纤维针织物碱减量开纤和染色研究

研究了裂片型超细纤维针织物碱减量开纤和染色。实验结果表明,失重率随时间延长而增加,当温度高于90℃、NaOH浓度高于8g/L时,失重率明显增加;在高于140℃对纤维热定型,失重率随温度升高而降低,当热定型温度高于180℃,开纤困难;纤维在染色后发现,K/S随纤维失重率增大而变小:用分散/阳离子染料或分散/酸性染料套染使K/S值有所提高;超细纤维在染色温度超过120℃时K/S值降低,温度越高,比普通涤纶的K/S差值越大     

分散染料可染丙纶的染色工艺

对影响分散染料可染丙纶上色率的染液浓度、浴比、固色时间、温度等工艺条件进行了试验 ,得到了较佳的染色工艺 :染液浓度 1.0 % (对织物质量 )、固色时间 90 min、温度 10 5℃、浴比 1∶ 5 0 ;分散染料可染丙纶长丝的上色率高于 PP/PET织物上色率。     

欧盟公布染料化学名称

该文根据欧盟2000年公布的第五版和2002年公布的第六版《欧洲化学物质申报清单》，选择一些重要的染料品种，介绍了他们的化学名称，以及可供参考的结构式。     

An efficient method for creation and functional analysis of libraries of hybrid type I polyketide synthases

Bacterial type I polyketide synthases (PKSs) generate a structurally diverse group of natural products with a wide range of biological activities. Hybrid type I PKSs in which domains of one multifunctional polypeptide are replaced with components from heterologous systems have generated significant interest over the past decade. Almost invariably only one or several specific hybrids are made at a time and tested for functionality. This approach is slow, dependent upon a fortuitous choice of specific fusions points, and often leads to inactive or minimally active hybrid systems. We describe herein a method for generating and screening a library of hybrid pikAI complementation plasmids (encoding the loading domain and the first two extension domains of pikromycin PKS) able to restore pikromycin in a BB138 Streptomyces venezuelae pikAI-deletion mutant. In the first step the plasmid sequence encoding the loading domain AT(0)-ACP(0) was replaced by a counter selectable marker, sacB. DNA family shuffling was then used to generate a diverse library of chimeric AT(0)-ACP(0) fragments, which were used to replace sacB by lambda-Red-mediated in vivo recombination in an Escherichia coli host. This method resulted in the rapid and efficient generation of a large number of hybrid pikAI complementation plasmids, which were used to transform S.venezuelae BB138. A bioassay of over 4000 of these transformants successfully revealed three different PikAI hybrids which were able to lead to pikromycin production. The study suggests that most of the hybrids are not detectably functional, and underscores the need to generate and screen large and diverse libraries in which different fusion points are tried. The methodologies applied in this study address this need and can be used for directed evolution of any component of the PikPKS, and potentially other type I PKS systems.     

Effect of protein fusion on the transition temperature of an environmentally responsive elastin-like polypeptide: a role for surface hydrophobicity?

The limited throughput, scalability and high cost of protein purification by chromatography provide motivation for the development of non-chromatographic protein purification technologies that are cheaper and easier to implement in a high-throughput format for proteomics applications and to scale up for industrial bioprocessing. We have shown that genetic fusion of a recombinant protein to an elastin-like polypeptide (ELP) imparts the environmentally sensitive solubility property of the ELP to the fusion protein, and thereby allows selective separation of the fusion protein from Escherichia coli lysate by aggregation above a critical temperature (T(t)). Further development of ELP fusion proteins as widely applicable purification tools necessitates a quantitative understanding of how fused proteins perturb the ELP T(t) such that purification conditions (T(t)) may be predicted a priori for new recombinant proteins. We report here the effect that fusing six different proteins has on the T(t) of an ELP. A negative correlation between T(t) and the fraction hydrophobic surface area on the fused proteins was observed, which was determined from computer modeling of the available three-dimensional structure. The thermally triggered aggregation behavior of ELP-coated, functionalized gold colloids as well as ligand binding to the tendamistat-ELP fusion protein support the hypothesis that hydrophobic surfaces in molecular proximity to ELPs depress the ELP T(t) by a mechanism analogous to hydrophobic residue substitution in the ELP repeat, Val-Pro-Gly-Xaa-Gly.     

Determination of Algerian Hassi-Messaoud asphaltene aromaticity with different solid-state NMR sequences

Algerian oil well deposit derived asphaltene fraction was characterized by different MAS/NMR sequences to investigate asphaltene aromaticity and the best cross-polarization contact time. The aromaticity was estimated by single pulse sequence (SP), Hahn-echo (HE), cross-polarization (CP) and variable cross-polarization (VACP) sequences. The values found ranging from 0.58 to 0.48 are of the same order of magnitude as ones published in the literature. The discrepancies between the values are thought to be relevant to both the specificity of each sequence and the asphaltene structure. Spectra band de-convolution enables us the determination of the average number of carbon atoms per side chain according to each sequence. The obtained values spanning from 3 to 7 are also sequence nature dependent.     

A novel emulsion mixture for in vitro compartmentalization of transcription and translation in the rabbit reticulocyte system

Emulsion formulations used for in vitro compartmentalization (IVC) methods were found to be incompatible with protein expression in the rabbit reticulocyte (RRL) system, causing rapid discoloration and translation shutdown. Here we identify possible causes and describe a novel water-in-oil emulsion which abolished discoloration and allowed high-level in-emulsion expression of active luciferase and human telomerase using the RRL. This novel emulsion greatly expands the range of potential protein targets for IVC.     

Conservation and covariance in PH domain sequences: physicochemical profile and information theoretical analysis of XLA-causing mutations in the Btk PH domain

Mutations that cause X-linked agammaglobulinemia (XLA) appear throughout the Bruton tyrosine kinase (Btk) sequence, including the pleckstrin homology (PH) domain. To analyze the basis of this disease with respect to protein structure, we studied the relationships between PH domain sequences and structures by comparing sequence-based profiles of physicochemical properties and solvent accessibility profiles. The diversity of the distribution of amino acids was measured by calculating entropies for sequences containing mutations at different positions in multiple sequence alignments. Mutual information was calculated to quantify positional covariation. Eight conserved extrema were apparent in all profiles. The majority of the XLA disease-causing mutations in the Btk PH domain were found at positions having significant mutual information, indicating that there are covariant constraints for both structure and function. Together with additional structural analyses, all the XLA mutations that were analyzed could be explained at the molecular level. The method developed here is applicable to the design of mutations for protein engineering.     

Identification of potent human anti-IL-1RI antagonist antibodies

Interleukin-1 (IL-1) blockade by IL-1 receptor antagonist benefits some arthritis patients by reducing joint damage. This fact inspired us to develop antagonist human therapeutic antibodies against IL-1R(I) using phage libraries that display single-chain variable fragment (scFv) antibody fragments. Panning libraries against human IL-1R(I) generated 39 unique scFv-phage whose binding to IL-1R(I) was competed by IL-1 ligands. Fifteen of these scFv-phage, identified using IL-1R(I)-binding assays and dissociation rate ranking, were reformatted as scFv-Fc and IgG(4) molecules. The ease of producing antibodies in the scFv-Fc format permitted rapid identification of four lead clones (C10, C13, C14, C15) that inhibit NF-kappaB nuclear translocation induced by IL-1. Reformatting these clones as IgG(4) molecules increased their inhibition potency by 相似文献   

Fusion of the antiferritin antibody VL domain to barnase results in enhanced solubility and altered pH stability

Chimeric immunotoxins that combine antigen recognition domains of antibodies and cytotoxic RNases have attracted much attention in recent years as potential targeted agents for cancer immunotherapy. In an attempt to obtain a structurally minimized immunofusion for folding/stability studies, we constructed the chimeric protein VL-barnase. The chimera comprises a small cytotoxic enzyme barnase, ribonuclease from Bacillus amyloliquefaciens, fused to the C-terminus of the light chain variable domain (VL) of the anti-human ferritin monoclonal antibody F11. While the individual VL domain was expressed in Escherichia coli as insoluble protein packed into inclusion bodies, its fusion to barnase resulted in a significant ( approximately 70%) fraction of soluble protein, with only a minor insoluble fraction ( approximately 30%) packed into inclusion bodies. The in vivo solubilizing effect of barnase was also observed in vitro and suggests a chaperone-like role that barnase exerted with regard to the N-terminal VL domain. Cytoplasmic VL-barnase was analyzed for structural and functional properties. The dimeric state of the chimeric protein was demonstrated by size-exclusion chromatography, thus indicating that fusion to barnase did not abrogate the intrinsic dimerization propensity of the VL domain. Ferritin-binding affinity and specificity in terms of constants of association with isoferritins were identical for the isolated VL domain and its barnase fusion, and RNase activity remained unchanged after the fusion. Intrinsic fluorescence spectra showed a fully compact tertiary structure of the fusion protein. However, significantly altered pH stability of the fusion protein versus individual VL and barnase was shown by the pH-induced changes in both intrinsic fluorescence and binding of ANS. Together, the results indicate that VL-barnase retained the antigen-binding affinity, specificity and RNase activity pertinent to the two individual constituents, and that their fusion into a single-chain chimeric protein resulted in an altered tertiary fold and pH stability.     

A cell-based screen for function of the four-helix bundle protein Rop: a new tool for combinatorial experiments in biophysics

Combinatorial methodologies have revolutionized studies in biomolecular function, but they have so far proven less useful for understanding macromolecular structure and stability. This is largely because of the difficulty of screening libraries of molecules for biophysical properties, and the difficulty of interpreting structural effects in complicated molecules. Here, we report a novel, robust, cell-based screen for function of the four-helix bundle protein, Rop. By expression of green fluorescent protein from a ColE1 plasmid, the screen reports the copy number of the plasmid, which is modulated in Escherichia coli by Rop. We have engineered the screen so that the fluorescent phenotype can correspond to either Rop activity or lack thereof. We have used the screen to demonstrate with systematically constructed Rop core variants that not all molecules that bind small stem-loop RNAs in vitro are active in vivo. Rop is well understood from structural work and systematic mutations, which makes it possible to construct rational, targeted libraries. This screen makes it possible to rapidly interrogate such libraries effectively for proper protein folding and stability. In addition to its intended utility for combinatorial experiments in biophysics, the screen will allow further dissection of the mechanism of Rop-mediated plasmid copy number regulation in vivo.