The third edition of this classic guide to protein purification updates methods, principles and references. As in the widely-acclaimed earlier editions, Scopes guides both the novice and the experienced researcher from theory to application. Using the book, the reader is able to integrate methods effectively into optimum protocols for the task at hand. Reviews of earlier editions: "good practical advice that is presented in a pleasantly readable form"--Analytical Biochemistry "well organized and written clearly" --American Scientist "should be on every laboratory shelf where protein are being handled or purified ... a feast and a genuine pleasure to read" --Nature.
"This updated edition of a widely accepted textbook now also includes discussions of the important techniques of high performance liquid chromatography and dye-ligand chromatography. The book is a practical guide on how to get started in planning a protein isolation and provides enough information to permit an intelligent choice of appropriate techniques. By pointing to more detailed information in the literature, it can also act as a reference book. This textbook is aimed at courses in protein purification in biochemistry and downstream processing in biotechnology."
"The enzyme purification laboratory; Making an extract; Separation by precipitation; Separation by adsorption; Separation in solution; Maintenance of active enzymes; Optimization of procedures and following a recipe; Measurement of enzyme activity; Analysis for purity; Crystallization; Solutions for measuring protein concentration."
"A guide providing a brief account of the main protein fractionation methods, with some simple theoretical and thermodynamic explanations of the events occurring, for students and researchers involved in the process of isolating an enzyme, from whatever source. A basic background in biochemistry and protein chemistry is assumed."
"The protein purification laboratory; Making an extract; Analysis - Measurement of protein and enzyme activity; Separation by precipitation; Separation by adsorption I: general principles; Separation by adsorption II: ion exchangers and nonspecific adsorbents; Separation by adsorption - affinity techniques; Separation in solution; Purification of special types of proteins; Small-scale and large-scale procedures; Analysis for purity; Optimization of procedures; Final Steps; Precipitation tables; Solutions for measuring protein concentration; Buffers for use in protein chemistry; Chromatographi materials."
"The enzyme purification laboratory; Making an extract; Separtion by precipitation; Separation by adsorption. II. specific adsorbents; Separtion in solution; Optmization of procedures, recombinant protein techniques; Maintenance of active enzymes; Measurement of enzyme activity; Analysis for purity."
"The third edition of this classic guide to protein purification updates methods, principles and references. As in the widely-acclaimed earlier editions, Scopes guides both the novice and the experienced researcher from theory to application. Using the book, the reader is able to integrate methods effectively into optimum protocols for the task at hand. Reviews of earlier editions: "good practical advice that is presented in a pleasantly readable form"--Analytical Biochemistry "well organized and written clearly" --American Scientist "should be on every laboratory shelf where protein are being handled or purified ... a feast and a genuine pleasure to read" --Nature."@en
"The enzyme purification laboratory. Apparatus, special materials, and particulate material. Principles of collumn chromatography. Manipulation of protein solutions. Making an extract. The raw material. Cell disintegration and extraction. Optimization and clarification of the extract. Procedures for particulate-associated enzymes. Separation by precipitation. General observations. The solubility of proteins ar low salt concentrations. Salting out at high salt concentrations. Precipitation with organic solvents. Precipitation with organic polymers and other materials; affinity precipitation. Precipitation by selective denuration. Separation by adsorption. I.general principles. General chromatographic theory. Batch adsorption. High-performance liquid chromatography: theory. Separation by adsorption.II. specific adsorbents. Ion exchangers-principles, properties, and uses. Ion-exchange chromatography: practical aspects. Affinity adsorption chromatography. Dye ligand chromatography. Affinity elution from ion exchangers and other nonspecificadsorbents. Immunoadsorbents. Miscellaneous adsoubents. Preparation insolution. Gel filtration. Electrophoretic methods-simple electrophoresis. Isoelectric focusing and isotachophoresis. Liquid phase partitioning. Ultrafiltration. Optimization or procedures; recombinant protein techniques. speed versus resulotion; the time factor. Scaling up and scaling down. Following a published procedure. Recombinant proteins-special techniques. Maintanence of active enzymes. Control of pH buffers. Stablizing factors for enzymes. Measurement of enzyme activity. Basic features of enzymic catalysis. Measurement of activity using stopped methods. Measurement of activity using continuous methods. Practical points in enzyme activity determination. Methods for measuring protein concentration. Analysis for purity: crystalization. Electrophorestic analysis. Other analytical methods. Crystalization of proteins."
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