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By Philip Bonner, Philip L.R. Bonner
Series: THE BASICS (Garland Science)
Protein Purification provides a guide to the major techniques, including non-affinity absorption techniques, affinity procedures, non-absorption techniques and methods for monitoring protein purity. There is an overview of protein strategy and equipment, followed by discussions and examples of each...
Published February 14th 2007 by Taylor & Francis
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string(1103) "ADVANTAGES ACTIVITY TANGENTIAL WHAT PROTEASE NON STAGE TECHNIQUES GROUND PSUPPLIERS DIFFERENT CENTRIFUGATION PROTEINS LIMITATIONS ESTABLISH PTHE SONICATION USED INTERACTION POLYETHYLENE HYDROPHOBIC METHODS GEL HYDROPHOBICITY MR INCLUDE STRATEGY REMOVAL PTECHNIQUES PRESS LYOPHILISATION CELLULAR WORK TEMPERATURE PPURIFICATION SCREENING EQUIPMENT INCLUSION PUSE PURIFIED P CONDITIONS SULPHATE AMMONIUM CLARIFICATION PROTEIN FLOW SPECIFIC BASICS ION MATERIAL USE BIOSPECIFICITY STABILITY IMMOBILISED SIMPLE HELP PCHOICE BINDING PURPOSES IMMUNO EXPLOITED ELUTION PROPERTIES TOTAL FRENCH PSTRONGCHAPTER UTILISED PREVIEW IMPORTANCE ULTRAFILTRATION EXPERIMENTS MAY ENZYME CENTRIFUGAL STRUCTURE POUTLINE CAN GETTING SYSTEMS STORAGE SOLVENTS THEM HETEROLOGOUS PURIFICATION HOMOGENISATION EXCHANGE EXPRESSION CHOICE VARIOUS DETERGENTS AFFINITY TE ASSAY GLYCOL PURIFY EXTRACTION DEBRIS INTEREST PMETHODS PURPOSE RESINS PERMEATION PSTRONG METAL COLUMNS BALANCE INHIBITORS STARTED CONCENTRATION CHARGE NBSP BUFFERS STRONG STARTING PEXTRACTION CHROMATOGRAPHY APPROPRIATE SHEET DIFFERENTIAL ABSORPTION INCLUDING PWHAT"
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