Preparative biochemistry最新文献_第4页

Interaction of bovine ceruloplasmin with erythrocytes. 牛铜蓝蛋白与红细胞的相互作用。

Preparative biochemistry Pub Date : 1994-05-01 DOI: 10.1080/10826069408010089

A C Fischer, C A Goode

引用次数: 1

Purification and biological activity of a recombinant human erythropoietin produced by lymphoblastoid cells. 淋巴母细胞样细胞产生的重组人红细胞生成素的纯化及生物活性研究。

Preparative biochemistry Pub Date : 1994-05-01 DOI: 10.1080/10826069408010087

A Ben Ghanem, J J Winchenne, C Lopez, S Chrétien, M Dubarry, C T Craescu, J P Le Caer, N Casadevall, P Rouger, J P Cartron

{"title":"Purification and biological activity of a recombinant human erythropoietin produced by lymphoblastoid cells.","authors":"A Ben Ghanem, J J Winchenne, C Lopez, S Chrétien, M Dubarry, C T Craescu, J P Le Caer, N Casadevall, P Rouger, J P Cartron","doi":"10.1080/10826069408010087","DOIUrl":"https://doi.org/10.1080/10826069408010087","url":null,"abstract":"A recombinant human erythropoietin (rH-EPO) was obtained from the culture supernatants of human B-lymphoblastoid cells transfected by the human EPO gene. rH-EPO was purified by a two-step method based on immunoaffinity and ion exchange chromatography. The first step was achieved by an anti-EPO monoclonal antibody (Mab). This Mab, immobilized on Sepharose 4B, allowed a 410-fold purification of the protein. The second step consisted of ion exchange chromatography on DEAE Sephacel. The combination of these two steps results in a highly purified rH-EPO with a global yield of about 50%; the specific activity of the protein was 176,000 IU/A280. The NMR spectrum was characteristic for a well structured, single-conformation protein. The purified protein was analyzed by SDS-PAGE and isoelectric focusing. The biological activity of purified rH-EPO was measured in vivo, by the incorporation of 59Fe into red blood cells (RBC) of polycythemic mice and in vitro by the proliferative response of an EPO-dependent cell line. The purified protein expressed in lymphoblastoid cells of human origin had the same biological activity as that of urinary EPO and rH-EPO produced in other mammalian cells.","PeriodicalId":20391,"journal":{"name":"Preparative biochemistry","volume":"24 2","pages":"127-42"},"PeriodicalIF":0.0,"publicationDate":"1994-05-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1080/10826069408010087","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"19067028","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: 14

Isolation of a polysaccharide with antiviral effect from Ulva lactuca. 一种具有抗病毒作用的枸杞多糖的分离。

Preparative biochemistry Pub Date : 1994-05-01 DOI: 10.1080/10826069408010084

V Ivanova, R Rouseva, M Kolarova, J Serkedjieva, R Rachev, N Manolova

引用次数: 99

Purification and characterization of acute phase rat plasma thiostatin. 急性期大鼠血浆硫抑素的纯化及特性研究。

Preparative biochemistry Pub Date : 1994-02-01 DOI: 10.1080/10826069408010081

M E Rusiniak, P V Wagh, G S Bedi, N Back

引用次数: 1

Recovery of lysozyme from scallop waste. 从扇贝废料中回收溶菌酶。

Preparative biochemistry Pub Date : 1994-02-01 DOI: 10.1080/10826069408010083

B Myrnes, A Johansen

引用次数: 31

A simple and efficient method for the purification of seminal plasmin, an antimicrobial protein from bovine seminal plasma. 一种从牛精浆中纯化精浆蛋白的简单有效方法。

Preparative biochemistry Pub Date : 1994-02-01 DOI: 10.1080/10826069408010079

D B Kameswari, K S Prasad

引用次数: 1

Optimization of synthesis of agarose-based lectin affinity sorbents. 琼脂糖基凝集素亲和吸附剂的合成优化。

Preparative biochemistry Pub Date : 1994-02-01 DOI: 10.1080/10826069408010082

M Lepiku, J Järv

引用次数: 0

Fractionation of carcinoembryonic antigen and related antigens in normal adult feces using a gradient medium Percoll. 用梯度培养基分离正常成人粪便中的癌胚抗原及相关抗原。

Preparative biochemistry Pub Date : 1994-02-01 DOI: 10.1080/10826069408010080

M Kuroki, M Kuwahara, M Murakami, Y Matsumoto, Y Matsuoka

引用次数: 1

Goat immunoglobulin purification on phosphocellulose and DEAE Affi-Gel blue. 山羊免疫球蛋白在磷纤维素和DEAE亲和凝胶蓝上的纯化。

Preparative biochemistry Pub Date : 1994-02-01 DOI: 10.1080/10826069408010078

P Ninfali, L Baronciani, S Rapa, D Marzioni, F Mannello

引用次数: 13

Improved chromatographic purification of peroxidase and beta-glucosidase from Hordeum vulgare seedlings. 改进的层析法纯化普通Hordeum幼苗过氧化物酶和β -葡萄糖苷酶。

Preparative biochemistry Pub Date : 1993-11-01 DOI: 10.1080/10826069308544571

A Rescigno, E Sanjust, N Curreli, A Padiglia, G Floris

{"title":"Improved chromatographic purification of peroxidase and beta-glucosidase from Hordeum vulgare seedlings.","authors":"A Rescigno, E Sanjust, N Curreli, A Padiglia, G Floris","doi":"10.1080/10826069308544571","DOIUrl":"https://doi.org/10.1080/10826069308544571","url":null,"abstract":"Peroxidases (E.C. 1.11.1.7., hydrogen donor oxidoreductase) utilize hydrogen peroxide or substituted peroxides for the oxidation of a large number of substrates. Peroxidases are widely distributed and have been isolated from many higher plants (1). The wide distribution of the enzyme suggests that it could be of great biological importance, but the physiological functions and metabolic control of these enzymes are still poorly understood. The simultaneous presence of amine oxidase and peroxidase in cell walls suggests that the peroxide generated on oxidation of the amines could be utilized by the peroxidase (2,3). Recently we have purified an amine oxidase from Hordeum vulgare (4) and we have attempted to purify the peroxidase in order to study in vitro the reconstituted coupled system. beta-glucosidase (beta-D-glucoside glucohydrolase E.C. 3.2.1.21.) is capable of transforming glucosides in glucose and the corresponding aglycone or disaccharides as cellobiose, sophorose, gentiobiose. This enzyme is widely distributed in plants, fungi, bacteria, yeasts and animals (5,6). In the homogenate of Hordeum vulgare seedlings we also found beta-glucosidase activity and also attempted to purify beta-glucosidase. This enzyme copurified with peroxidase up to the last step. We report here the isolation of peroxidase and beta-glucosidase from Hordeum vulgare seedlings: some molecular and kinetic properties are given.","PeriodicalId":20391,"journal":{"name":"Preparative biochemistry","volume":"23 4","pages":"485-92"},"PeriodicalIF":0.0,"publicationDate":"1993-11-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1080/10826069308544571","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"19235825","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: 10