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Preparative biochemistry最新文献

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Preparative purification of pig red blood cell hexokinase type III using a new efficient chromatographic support. 新型高效色谱载体制备纯化猪红细胞己糖激酶III型。
Preparative biochemistry Pub Date : 1992-03-01 DOI: 10.1080/10826069208018018
V Stocchi, L Masat, B Biagiarelli, G Piccoli, F Palma, L Cucchiarini, M Dachà
{"title":"Preparative purification of pig red blood cell hexokinase type III using a new efficient chromatographic support.","authors":"V Stocchi,&nbsp;L Masat,&nbsp;B Biagiarelli,&nbsp;G Piccoli,&nbsp;F Palma,&nbsp;L Cucchiarini,&nbsp;M Dachà","doi":"10.1080/10826069208018018","DOIUrl":"https://doi.org/10.1080/10826069208018018","url":null,"abstract":"<p><p>In this paper we report the purification of pig erythrocyte hexokinase type III, at preparative level, using 52 liters of starting material (hemolysate). This was possible using a new efficient anion exchanger support, the Toyopearl DEAE 650 M which allows completely to change the strategy of removing hemoglobin from hemolysates, permitting to handle large amounts of starting material and reducing work would have required months using conventional anion exchanger supports, to only 2-3 days. Furthermore, we have tested the binding of other red blood cell enzymes to the Toyopearl DEAE 650 M, showing a wider potential use of this chromatographic support for their purification at a preparative level.</p>","PeriodicalId":20391,"journal":{"name":"Preparative biochemistry","volume":"22 1","pages":"41-51"},"PeriodicalIF":0.0,"publicationDate":"1992-03-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1080/10826069208018018","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"12787437","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
High resolution of multiple forms of red blood cell enzymes using a Toyopearl DEAE 650 S. 高分辨率的多种形式的红细胞酶使用丰田公司deae650s。
Preparative biochemistry Pub Date : 1992-03-01 DOI: 10.1080/10826069208018017
V Stocchi, L Masat, B Biagiarelli, A Accorsi, G Piccoli, F Palma, L Cucchiarini, M Dachà
{"title":"High resolution of multiple forms of red blood cell enzymes using a Toyopearl DEAE 650 S.","authors":"V Stocchi,&nbsp;L Masat,&nbsp;B Biagiarelli,&nbsp;A Accorsi,&nbsp;G Piccoli,&nbsp;F Palma,&nbsp;L Cucchiarini,&nbsp;M Dachà","doi":"10.1080/10826069208018017","DOIUrl":"https://doi.org/10.1080/10826069208018017","url":null,"abstract":"<p><p>We have investigated a new anion exchange chromatographic support (Toyopearl DEAE 650 S) which simultaneously allows easily to remove hemoglobin from hemolysates and to obtain a very high resolution of enzymes present in multiple forms. The results obtained are better than those obtainable using an anion-exchange HPLC column. The data obtained at analytical level suggest a wider use of this new matrix also for preparative purposes without significant changes in the resolution.</p>","PeriodicalId":20391,"journal":{"name":"Preparative biochemistry","volume":"22 1","pages":"11-40"},"PeriodicalIF":0.0,"publicationDate":"1992-03-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1080/10826069208018017","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"12787436","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
Purifying nuclei. 净化核。
Preparative biochemistry Pub Date : 1992-03-01 DOI: 10.1080/10826069208018016
R Jakob
{"title":"Purifying nuclei.","authors":"R Jakob","doi":"10.1080/10826069208018016","DOIUrl":"https://doi.org/10.1080/10826069208018016","url":null,"abstract":"<p><p>Nuclear isolation methods exist since over 50 years and even today new procedures and amendments of standard methods are published. They can be classified into nonaqueous and aqueous methods. The latter can be subdivided into isotonic, hypertonic and hypotonic systems. In most cases the aqueous isolation renders nuclei closer to their physiological status in the cell. A standard method for the hypotonic isolation of nuclei is presented and the methodology of nuclear isolation is discussed.</p>","PeriodicalId":20391,"journal":{"name":"Preparative biochemistry","volume":"22 1","pages":"1-9"},"PeriodicalIF":0.0,"publicationDate":"1992-03-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1080/10826069208018016","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"12787435","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
Large scale extraction of alpha-lactalbumin and beta-lactoglobulin from bovine whey by precipitation with polyethylene glycol and partitioning in aqueous two-phase systems. 聚乙二醇沉淀法和双水相分离法从牛乳清中大规模提取α -乳清蛋白和β -乳球蛋白。
Preparative biochemistry Pub Date : 1992-03-01 DOI: 10.1080/10826069208018019
A Ortín, J A Cebrian, G Johansson
{"title":"Large scale extraction of alpha-lactalbumin and beta-lactoglobulin from bovine whey by precipitation with polyethylene glycol and partitioning in aqueous two-phase systems.","authors":"A Ortín,&nbsp;J A Cebrian,&nbsp;G Johansson","doi":"10.1080/10826069208018019","DOIUrl":"https://doi.org/10.1080/10826069208018019","url":null,"abstract":"<p><p>The milk proteins alpha-lactalbumin and beta-lactoglobulin have been isolated from bovine whey by fractional precipitation with polyethylene glycol (PEG) and hydrophobic partitioning in aqueous PEG-hydroxypropylstarch two-phase systems using PEG-bound palmitate as hydrophobic ligand. The possible use of this combination for large scale purification of these whey proteins is discussed.</p>","PeriodicalId":20391,"journal":{"name":"Preparative biochemistry","volume":"22 1","pages":"53-66"},"PeriodicalIF":0.0,"publicationDate":"1992-03-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1080/10826069208018019","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"12787438","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: 6
Purification and characterization of kallikrein-like serine proteases from rat submandibular glands. 大鼠颌下腺钾化钾素样丝氨酸蛋白酶的纯化与特性研究。
Preparative biochemistry Pub Date : 1992-03-01 DOI: 10.1080/10826069208018020
G S Bedi
{"title":"Purification and characterization of kallikrein-like serine proteases from rat submandibular glands.","authors":"G S Bedi","doi":"10.1080/10826069208018020","DOIUrl":"https://doi.org/10.1080/10826069208018020","url":null,"abstract":"<p><p>The purification and characterization of kallikrein-like proteases from rat submandibular glands is described. The proteolytic activity of each fraction during purification was monitored on the synthetic substrate N-alpha-tosyl-L-arginine methyl ester (TAME). The purification scheme involved ammonium sulfate precipitation, chromatography on columns of DEAE-Sepharose and Sephadex G-100 and chromatofocusing. Three TAME-hydrolytic activity peaks were eluted from DEAE-Sepharose as unbound fraction (Pool 1), at 125 mM NaCl (Pool 2) and at 250 mM NaCl concentration (Pool 4). Pool 1 further resolved into two protease fractions (1A1 and 1A2), pool 2 into three protease fractions (2A1, 2A2 and 2A3) and pool 4 gave a single major protease peak (4A1) by chromatofocusing on PBE-94. Protease pools 2A2, 2A3, and 4A1 each gave a single band on SDS-polyacrylamide gel electrophoresis with an estimated molecular weight of 34 kDa, 46 kDa and 46 kDa respectively. Pools 1A1, 1A2, 2A1 and 2a2 gave a single precipitin line with anti-rat glandular kallikrein antibodies. 2A3 and 4A1 did not react with these antibodies. Synthetic substrates DL-val-leu-arg-pNA and Bz-pro-phe-arg-pNA, specific for kallikrein-like proteases, were hydrolyzed preferentially by 2A3 and 4A1 but were poor substrates for 1A1, 1A2, 2A1 and 2A2.</p>","PeriodicalId":20391,"journal":{"name":"Preparative biochemistry","volume":"22 1","pages":"67-81"},"PeriodicalIF":0.0,"publicationDate":"1992-03-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1080/10826069208018020","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"12787439","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: 6
The affinity purification and characterization of a dehydrogenase from Aspergillus parasiticus involved in aflatoxin B1 biosynthesis. 参与黄曲霉毒素B1合成的寄生曲霉脱氢酶的亲和纯化及特性研究。
Preparative biochemistry Pub Date : 1991-01-01 DOI: 10.1080/10826069108018008
A A Chuturgoon, M F Dutton
{"title":"The affinity purification and characterization of a dehydrogenase from Aspergillus parasiticus involved in aflatoxin B1 biosynthesis.","authors":"A A Chuturgoon,&nbsp;M F Dutton","doi":"10.1080/10826069108018008","DOIUrl":"https://doi.org/10.1080/10826069108018008","url":null,"abstract":"<p><p>A two step scheme has been developed for the purification of a dehydrogenase from mycelia of 84 hours old Aspergillus parasiticus (1-11-105 Wh 1), which catalyzes the conversion of norsolorinic acid (NA) to averantin (AVN). The dehydrogenase was purified from cell-free extracts using reactive green 19-agarose and norsolorinic acid-agarose affinity chromatography. The latter affinity matrix was synthesised by attaching norsolorinic acid to omega-aminohexylagarose. The purified protein was shown to be homogenous on non-denaturing polyacrylamide gel electrophoresis. A final purification of 215-fold was achieved. Results of gel filtration chromatography indicated the approximate molecular mass of the native protein to be 140,000 daltons. The isoelectric point of the protein was about 5.5 as determined by chromatofocusing. The reaction catalyzed by the dehydrogenase was optimum at pH 8.5 and between 25 degrees to 35 degrees C. The Km of the enzyme for NA and NADPH was determined to be 3.45 microM and 103 microM respectively.</p>","PeriodicalId":20391,"journal":{"name":"Preparative biochemistry","volume":"21 2-3","pages":"125-40"},"PeriodicalIF":0.0,"publicationDate":"1991-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1080/10826069108018008","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"12960227","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
Purification of ferredoxin-NADP+ reductase, flavodoxin and ferredoxin from a single batch of the cyanobacterium Anabaena PCC 7119. 赤潮蓝藻PCC 7119中铁氧还蛋白- nadp +还原酶、黄氧还蛋白和铁氧还蛋白的纯化。
Preparative biochemistry Pub Date : 1991-01-01 DOI: 10.1080/10826069108018571
J J Pueyo, C Gómez-Moreno
{"title":"Purification of ferredoxin-NADP+ reductase, flavodoxin and ferredoxin from a single batch of the cyanobacterium Anabaena PCC 7119.","authors":"J J Pueyo,&nbsp;C Gómez-Moreno","doi":"10.1080/10826069108018571","DOIUrl":"https://doi.org/10.1080/10826069108018571","url":null,"abstract":"<p><p>Methods are described for the simultaneous isolation of ferredoxin-NADP+ reductase, ferredoxin and flavodoxin from large quantities of the cyanobacterium Anabaena PCC 7119 allowing the use of a single batch of cells. The ultraviolet-visible spectra and the extinction coefficients of ferredoxin-NADP+ reductase and ferredoxin were determined. The purification procedure also yields enriched fractions of phycobiliproteins and cytochrome c553.</p>","PeriodicalId":20391,"journal":{"name":"Preparative biochemistry","volume":"21 4","pages":"191-204"},"PeriodicalIF":0.0,"publicationDate":"1991-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1080/10826069108018571","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"12829603","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: 41
Purification of prephenate dehydratase from Corynebacterium glutamicum by affinity chromatography. 亲和层析法纯化谷氨酸棒状杆菌中预苯酸脱水酶。
Preparative biochemistry Pub Date : 1991-01-01 DOI: 10.1080/10826069108018578
S Bertaux, R G Harrison
{"title":"Purification of prephenate dehydratase from Corynebacterium glutamicum by affinity chromatography.","authors":"S Bertaux,&nbsp;R G Harrison","doi":"10.1080/10826069108018578","DOIUrl":"https://doi.org/10.1080/10826069108018578","url":null,"abstract":"<p><p>Prephenate dehydratase has been purified from the wild type strain Corynebacterium glutamicum by affinity chromatography. Three ligands, L-Trp, L-Tyr, and L-Phe have been tested as well as conditions for elution. L-Phe is the most specific ligand: it leads to a purification factor of 11 in one step using step gradients of NaCl in Tris-HCl buffer at pH 7.5.</p>","PeriodicalId":20391,"journal":{"name":"Preparative biochemistry","volume":"21 4","pages":"269-75"},"PeriodicalIF":0.0,"publicationDate":"1991-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1080/10826069108018578","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"12942366","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: 3
A sensitive multienzymatic assay for the measurement of pyruvate, dihydroxyacetone phosphate, oxaloacetate, and acetoacetate in clear extracts from biological samples. 测定生物样品中丙酮酸、磷酸二羟丙酮、草酰乙酸和乙酰乙酸的一种灵敏的多酶分析方法。
Preparative biochemistry Pub Date : 1991-01-01 DOI: 10.1080/10826069108018573
F Arias-Mendoza, E Piña
{"title":"A sensitive multienzymatic assay for the measurement of pyruvate, dihydroxyacetone phosphate, oxaloacetate, and acetoacetate in clear extracts from biological samples.","authors":"F Arias-Mendoza,&nbsp;E Piña","doi":"10.1080/10826069108018573","DOIUrl":"https://doi.org/10.1080/10826069108018573","url":null,"abstract":"<p><p>A multienzymatic method for the measurement of pyruvate, dihydroxyacetone phosphate, oxaloacetate, and acetoacetate is presented. The determination procedure is considered suitable because it is simple, sensitive, and its advantages could be demonstrated by comparison with the original methods.</p>","PeriodicalId":20391,"journal":{"name":"Preparative biochemistry","volume":"21 4","pages":"211-4"},"PeriodicalIF":0.0,"publicationDate":"1991-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1080/10826069108018573","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"12942363","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: 3
Purification and properties of alpha-aminoadipate aminotransferase from rat liver and kidney mitochondria. 大鼠肝、肾线粒体α -氨基己二酸转氨酶的纯化及性质研究。
Preparative biochemistry Pub Date : 1991-01-01 DOI: 10.1080/10826069108018010
M R Mawal, A Mukhopadhyay, D R Deshmukh
{"title":"Purification and properties of alpha-aminoadipate aminotransferase from rat liver and kidney mitochondria.","authors":"M R Mawal,&nbsp;A Mukhopadhyay,&nbsp;D R Deshmukh","doi":"10.1080/10826069108018010","DOIUrl":"https://doi.org/10.1080/10826069108018010","url":null,"abstract":"<p><p>Recently we reported an affinity chromatography method to purify alpha-aminoadipate aminotransferase (AadAT) activity from rat kidney supernatant fraction. Using the same affinity column, we purified AadAT activities from rat kidney and liver mitochondria. The physical and kinetic properties such as pH optima, Km for substrates, molecular weight, subunit structure, isoelectric pH, electrophoretic mobility and inhibition by dicarboxylic acids of mitochondrial AadAT were similar to those of the AadAT from rat kidney supernatant fraction. These results indicate that AadAT from different subcellular fractions is structurally and immunologically identical.</p>","PeriodicalId":20391,"journal":{"name":"Preparative biochemistry","volume":"21 2-3","pages":"151-62"},"PeriodicalIF":0.0,"publicationDate":"1991-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1080/10826069108018010","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"12960228","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: 5
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