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High-speed pectic enzyme fractionation by immobilised metal ion affinity membranes. 固定化金属离子亲和膜的高速果胶酶分离。
Bioseparation Pub Date : 2000-01-01 DOI: 10.1023/a:1008187929132
S A Camperi, M Grasselli, O Cascone
{"title":"High-speed pectic enzyme fractionation by immobilised metal ion affinity membranes.","authors":"S A Camperi,&nbsp;M Grasselli,&nbsp;O Cascone","doi":"10.1023/a:1008187929132","DOIUrl":"https://doi.org/10.1023/a:1008187929132","url":null,"abstract":"<p><p>Immobilised metal ion affinity polysulfone hollow-fibre membranes, with a high capacity for protein adsorption, were prepared and their utilisation for commercial pectic enzyme fractionation was studied. The pass-through fraction containing pectinlyase is useful for fruit-juice clarification without methanol production on account of pectinesterase being retained by the IDA-Cu2+ membrane.</p>","PeriodicalId":9179,"journal":{"name":"Bioseparation","volume":"9 3","pages":"173-7"},"PeriodicalIF":0.0,"publicationDate":"2000-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1023/a:1008187929132","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"21929132","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
引用次数: 9
Improved purification of Candida boidinii formate dehydrogenase. 假丝酵母甲酸脱氢酶的改进纯化。
Bioseparation Pub Date : 2000-01-01 DOI: 10.1023/a:1008131320571
N E Labrou
{"title":"Improved purification of Candida boidinii formate dehydrogenase.","authors":"N E Labrou","doi":"10.1023/a:1008131320571","DOIUrl":"https://doi.org/10.1023/a:1008131320571","url":null,"abstract":"<p><p>Formate dehydrogenase (FDH, EC 1.2.1.2) from Candida boidinii was purified to homogeneity. The two step procedure comprised anion exchange chromatography (2.9-fold purification, 85% step yield, elution with 35 mM KCl), followed by dye-ligand affinity chromatography on immobilized Cibacron Blue 3GA (1.4-fold purification, 75% step yield, elution with 0.15 mM NAD+/2 mM Na2SO3). The procedure afforded FDH at 63.8% overall yield and a specific activity of 7.2 units/mg. The purity of the final FDH preparation was evaluated by sodium dodecyl sulphate polyacrylamide gel electrophoresis (SDS-PAGE), high performance gel filtration liquid chromatography (gfHPLC) and N-terminal amino acid sequencing. The analytical techniques showed the presence of a single polypeptide chain that corresponds to the molecular weight of 41 kDa (as determined by SDS-PAGE) and 81 kDa (as determined by gfHPLC).</p>","PeriodicalId":9179,"journal":{"name":"Bioseparation","volume":"9 2","pages":"99-104"},"PeriodicalIF":0.0,"publicationDate":"2000-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1023/a:1008131320571","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"21734413","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
引用次数: 11
Short cut of protein purification by integration of cell-disrupture and affinity extraction. 结合细胞破坏和亲和萃取纯化蛋白质的捷径。
Bioseparation Pub Date : 2000-01-01 DOI: 10.1023/a:1008135913202
M Schuster, E Wasserbauer, C Ortner, K Graumann, A Jungbauer, F Hammerschmid, G Werner
{"title":"Short cut of protein purification by integration of cell-disrupture and affinity extraction.","authors":"M Schuster,&nbsp;E Wasserbauer,&nbsp;C Ortner,&nbsp;K Graumann,&nbsp;A Jungbauer,&nbsp;F Hammerschmid,&nbsp;G Werner","doi":"10.1023/a:1008135913202","DOIUrl":"https://doi.org/10.1023/a:1008135913202","url":null,"abstract":"<p><p>Screening strategies based on functional genomics require the isolation of gene products of several hundred cDNA clones in a fast and versatile manner. Conventional purification strategies will fail to accomplish this goal within a reasonable time frame. In order to short-cut these procedures, we have developed a combination of cell disintegration and affinity technique for rapid isolation and purification. For our purpose, tagged proteins have been produced in yeast by fusing the FLAG-sequence adjacent to the 5' end of cDNAs coding for the respective protein. The example of an over-expressed FLAG-tagged fusion protein, human serum albumin (HSA), was released into the cytoplasm. Detection and purification of the FLAG-fusion protein were carried out by using a mouse monoclonal antibody directed against the FLAG-peptide. For purification purposes, the antibody was immobilized on PROSEP magnetic glass beads. These magnetic glass beads with 500 microns diameter have been investigated for disintegration of yeast and simultaneous capturing of the target protein. After 60 s, 90% of the maximal disintegration level was achieved when a ratio of 20 microliters yeast cell suspension and 100 microliters glass are vortexed. After a wash step, the FLAG-fusion proteins have been eluted with chelating agents such as EDTA. The short-cut procedure has been compared to a conventional purification strategy using an affinity chromatography process. Due to the highly favorable binding characteristics of the applied immunoaffinity sorbent the yield observed in batch operation was 90% and purity in the range of 70-80%.</p>","PeriodicalId":9179,"journal":{"name":"Bioseparation","volume":"9 2","pages":"59-67"},"PeriodicalIF":0.0,"publicationDate":"2000-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1023/a:1008135913202","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"21734507","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
引用次数: 22
Modern Techniques for Polymer Characterisation R.A. Pethrick & J.V. Dawkins (Eds.) 现代聚合物表征技术R.A. Pethrick & J.V. Dawkins(编)
Bioseparation Pub Date : 2000-01-01 DOI: 10.1023/A:1008179318150
J. Kennedy, M. Thorley
{"title":"Modern Techniques for Polymer Characterisation R.A. Pethrick & J.V. Dawkins (Eds.)","authors":"J. Kennedy, M. Thorley","doi":"10.1023/A:1008179318150","DOIUrl":"https://doi.org/10.1023/A:1008179318150","url":null,"abstract":"","PeriodicalId":9179,"journal":{"name":"Bioseparation","volume":"128 1","pages":"57-58"},"PeriodicalIF":0.0,"publicationDate":"2000-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"76558443","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
引用次数: 2
Observation of yeast cell movement and aggregation in a small-scale MHz-ultrasonic standing wave field 小尺度mhz -超声波驻波场中酵母细胞运动和聚集的观察
Bioseparation Pub Date : 2000-01-01 DOI: 10.1023/A:1011113826753
J. Spengler, M. Jekel, K. Christensen, R. Adrian, J. Hawkes, W. Coakley
{"title":"Observation of yeast cell movement and aggregation in a small-scale MHz-ultrasonic standing wave field","authors":"J. Spengler, M. Jekel, K. Christensen, R. Adrian, J. Hawkes, W. Coakley","doi":"10.1023/A:1011113826753","DOIUrl":"https://doi.org/10.1023/A:1011113826753","url":null,"abstract":"","PeriodicalId":9179,"journal":{"name":"Bioseparation","volume":"51 1","pages":"329-341"},"PeriodicalIF":0.0,"publicationDate":"2000-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"75149376","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
引用次数: 72
Sub-micron particle manipulation in an ultrasonic standing wave: Applications in detection of clinically important biomolecules 超声驻波中的亚微米粒子操纵:在临床重要生物分子检测中的应用
Bioseparation Pub Date : 2000-01-01 DOI: 10.1023/A:1011175404581
M. Sobanski, C. Robert Tucker, N. E. Thomas, W. Terence Coakley
{"title":"Sub-micron particle manipulation in an ultrasonic standing wave: Applications in detection of clinically important biomolecules","authors":"M. Sobanski, C. Robert Tucker, N. E. Thomas, W. Terence Coakley","doi":"10.1023/A:1011175404581","DOIUrl":"https://doi.org/10.1023/A:1011175404581","url":null,"abstract":"","PeriodicalId":9179,"journal":{"name":"Bioseparation","volume":"29 1","pages":"351-357"},"PeriodicalIF":0.0,"publicationDate":"2000-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"73957531","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
引用次数: 27
Crime Scene To Court Peter White (editor) 犯罪现场起诉彼得·怀特(编辑)
Bioseparation Pub Date : 2000-01-01 DOI: 10.1023/A:1008103128704
J. Kennedy, Lorraine A. Quinton
{"title":"Crime Scene To Court Peter White (editor)","authors":"J. Kennedy, Lorraine A. Quinton","doi":"10.1023/A:1008103128704","DOIUrl":"https://doi.org/10.1023/A:1008103128704","url":null,"abstract":"","PeriodicalId":9179,"journal":{"name":"Bioseparation","volume":"32 2 1","pages":"55-56"},"PeriodicalIF":0.0,"publicationDate":"2000-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"85939058","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
引用次数: 0
Efficient heterodimerization of recombinant bi- and trispecific antibodies. 重组双特异性和三特异性抗体的高效异源二聚化。
Bioseparation Pub Date : 2000-01-01 DOI: 10.1023/a:1008120203269
R Schoonjans, A Willems, J Grooten, N Mertens
{"title":"Efficient heterodimerization of recombinant bi- and trispecific antibodies.","authors":"R Schoonjans,&nbsp;A Willems,&nbsp;J Grooten,&nbsp;N Mertens","doi":"10.1023/a:1008120203269","DOIUrl":"https://doi.org/10.1023/a:1008120203269","url":null,"abstract":"<p><p>Bispecific antibodies (BsAb) are promising therapeutic tools in tomorrow's medicine. Expression systems favoring efficient heterodimerization of intermediate-sized bispecific antibodies will significantly improve existing production methods. By C-terminal fusion of scFv molecules to the Fd- and the L-chains efficient heterodimerization in mammalian cells was obtained and a novel intermediate sized, disulfide stabilized BsAb could be efficiently produced. This type of antibody derivative easily allows for the production of trispecific antibodies, BsAb with bivalent binding for one antigen, or immunoconjugates.</p>","PeriodicalId":9179,"journal":{"name":"Bioseparation","volume":"9 3","pages":"179-83"},"PeriodicalIF":0.0,"publicationDate":"2000-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1023/a:1008120203269","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"21928458","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
引用次数: 1
Purification, characterization and crystallization of enzymes for dibenzothiophene desulfurization. 二苯并噻吩脱硫酶的纯化、表征及结晶。
Bioseparation Pub Date : 2000-01-01 DOI: 10.1023/a:1008181730720
T Ohshiro, Y Izumi
{"title":"Purification, characterization and crystallization of enzymes for dibenzothiophene desulfurization.","authors":"T Ohshiro,&nbsp;Y Izumi","doi":"10.1023/a:1008181730720","DOIUrl":"https://doi.org/10.1023/a:1008181730720","url":null,"abstract":"<p><p>DszC and DszA, DBT monooxygenase and DBT sulfone monooxygenase, respectively, involved in dibenzothiophene (DBT) desulfurization, were purified to homogeneity from Rhodococcus erythropolis D-1. The two enzymes were crystallized and enzymologically characterized. We found a high activity of flavin reductase in the non-DBT-desulfurizing bacterium, Paenibacillus polymyxa A-1, which is essential for DszC and A activities, and purified to homogeneity and characterized the enzyme.</p>","PeriodicalId":9179,"journal":{"name":"Bioseparation","volume":"9 3","pages":"185-8"},"PeriodicalIF":0.0,"publicationDate":"2000-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1023/a:1008181730720","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"21928459","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
引用次数: 15
Pervaporative stripping of acetone, butanol and ethanol to improve ABE fermentation. 丙酮、丁醇和乙醇的透汽提提改善ABE发酵。
Bioseparation Pub Date : 2000-01-01 DOI: 10.1023/a:1008129713552
K Jitesh, V G Pangarkar, K Niranjan
{"title":"Pervaporative stripping of acetone, butanol and ethanol to improve ABE fermentation.","authors":"K Jitesh,&nbsp;V G Pangarkar,&nbsp;K Niranjan","doi":"10.1023/a:1008129713552","DOIUrl":"https://doi.org/10.1023/a:1008129713552","url":null,"abstract":"<p><p>Acetone-butanol-ethanol fermentation by anaerobic bacterium C. acetobutylicum is a potential source for feedstock chemicals. The problem of product induced inhibition makes this fermentation economically infeasible. Pervaporation is studied as an effective separation technique to remove the toxic inhibitory products. Various membranes like Styrene Butadiene Rubber (SBR), Ethylene Propylene Diene Rubber (EPDM), plain Poly Dimethyl Siloxane (PDMS) and silicalite filled PDMS were studied for the removal of acetone, butanol and ethanol, from binary aqueous mixtures and from a quaternary mixture. It was found that the overall performance of PDMS filled with 15% w/w of silicalite was the best for removal of butanol in binary mixture study. SBR performance was best for the quaternary mixture studied.</p>","PeriodicalId":9179,"journal":{"name":"Bioseparation","volume":"9 3","pages":"145-54"},"PeriodicalIF":0.0,"publicationDate":"2000-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1023/a:1008129713552","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"21929128","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
引用次数: 55
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