Use of rotofor preparative isoelectrofocusing cell in protein purification procedure

1998 ◽  
Vol 69 (1) ◽  
pp. 11-16 ◽  
Author(s):  
Antonio Ayala ◽  
Juan Parrado ◽  
Alberto Machado
2019 ◽  
Vol 153 ◽  
pp. 1-6 ◽  
Author(s):  
Wolfgang Becker ◽  
Anne Scherer ◽  
Christine Faust ◽  
David Kornblüh Bauer ◽  
Simone Scholtes ◽  
...  

2008 ◽  
Vol 59 (7) ◽  
Author(s):  
Ileana Vajiala ◽  
Ruxandra Subasu ◽  
Mirela Zorio ◽  
Rodica Picu

Upon screening identification of Stanozolol, GC/HRMS confirmation of the suspicious sample is done by reanalysis of the urine specimen, where a specific immunoaffinity purification procedure is used to selectively isolate the long term excreted metabolites of Stanozolol. By meeting the specific identification criteria for more than one metabolite of the same parent compound, additional evidence could be obtained in the decision making process in doping control.


2020 ◽  
Vol 21 (8) ◽  
pp. 821-830
Author(s):  
Vibhor Mishra

The affinity tags are unique proteins/peptides that are attached at the N- or C-terminus of the recombinant proteins. These tags help in protein purification. Additionally, some affinity tags also serve a dual purpose as solubility enhancers for challenging protein targets. By applying a combinatorial approach, carefully chosen affinity tags designed in tandem have proven to be very successful in the purification of single proteins or multi-protein complexes. In this mini-review, the key features of the most commonly used affinity tags are discussed. The affinity tags have been classified into two significant categories, epitope tags, and protein/domain tags. The epitope tags are generally small peptides with high affinity towards a chromatography resin. The protein/domain tags often perform double duty as solubility enhancers as well as aid in affinity purification. Finally, protease-based affinity tag removal strategies after purification are discussed.


1992 ◽  
Vol 57 (8) ◽  
pp. 1632-1638 ◽  
Author(s):  
Věra Tatarkovičová ◽  
Zdeněk Stránský

The procedure for the determination of carbamate pesticides in soil was optimized. The following factors affecting the final results were investigated: extracting solvent, extraction procedure, extract purification procedure, and soil type. Triple extraction with acetone and purification of the extract on a two-stage purification column containing an activated carbon-silica gel 1+1 mixture were found optimal. The extracts after treatment were analyzed by RP-HPLC with UV detection. The method developed allows carbamate pesticides in soil to be determined at concentrations in excess of 30 μg kg-1.


Proteins are an integral part of molecular and cellular structure and function and are probably the most purified type of biological molecule. In order to elucidate the structure and function of any protein it is first necessary to purify it. Protein purification techniques have evolved over the past ten years with improvements in equipment control, automation, and separation materials, and the introduction of new techniques such as affinity membranes and expanded beds. These developments have reduced the workload involved in protein purification, but there is still a need to consider how unit operations linked together to form a purification strategy, which can be scaled up if necessary. The two Practical Approach books on protein purification have therefore been thoroughly updated and rewritten where necessary. The core of both books is the provision of detailed practical guidelines aimed particularly at laboratory scale purification. Information on scale-up considerations is given where appropriate. The books are not comprehensive but do cover the major laboratory techniques and common sources of protein. Protein Purification Techniques focuses on unit operations and analytical techniques. It starts with an overview of purification strategy and then covers initial extraction and clarification techniques. The rest of the book concentrates on different purification methods with the emphasis being on chromatography. The final chapter considers general scale-up considerations. Protein Purification Applications describes purification strategies from common sources: mammalian cell culture, microbial cell culture, milk, animal tissue, and plant tissue. It also includes chapters on purification of inclusion bodies, fusion proteins, and purification for crystallography. A purification strategy that can produce a highly pure single protein from a crude mixture of proteins, carbohydrates, lipids, and cell debris to is a work of art to be admired. These books (available individually or as a set)are designed to give the laboratory worker the information needed to undertake the challenge of designing such a strategy.


1985 ◽  
Vol 260 (11) ◽  
pp. 7029-7034 ◽  
Author(s):  
R W Scott ◽  
B L Bergman ◽  
A Bajpai ◽  
R T Hersh ◽  
H Rodriguez ◽  
...  

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