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Jornitz, and Uwe Gottschalkġ3 Refolding of Inclusion Body Proteins from E. OTHER SEPARATION METHODS AND RELATED TECHNIQUES Jan-Christer Janson and Jan A˚ke Jo¨nssonģ Gel Filtration: Size Exclusion Chromatographyĥ High-Resolution Reversed-Phase Chromatography of Proteinsħ Immobilized Metal Ion Affinity Chromatographyįrancisco Batista-Viera, Lars Ryde´n, and Jan Carlssonįrancisco Batista-Viera, Jan-Christer Janson, and Jan Carlssonġ0 Affinity Ligands from Chemical Combinatorial Librariesġ1 Affinity Ligands from Biological Combinatorial Libraries 6-dc22 2010033316 Printed in the United States of America 10 9 8 7 6 5 4 3 2 1īo Ersson, Lars Ryde´n, and Jan-Christer Janson
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You should consult with a professional where appropriate. The advice and strategies contained herein may not be suitable for your situation. No warranty may be created or extended by sales representatives or written sales materials. Limit of Liability/Disclaimer of Warranty: While the publisher and author have used their best efforts in preparing this book, they make no representations or warranties with respect to the accuracy or completeness of the contents of this book and specifically disclaim any implied warranties of merchantability or fitness for a particular purpose. All rights reserved Published by John Wiley & Sons, Inc., Hoboken, New Jersey Published simultaneously in Canada No part of this publication may be reproduced, stored in a retrieval system, or transmitted in any form or by any means, electronic, mechanical, photocopying, recording, scanning, or otherwise, except as permitted under Section 107 or 108 of the 1976 United States Copyright Act, without either the prior written permission of the Publisher, or authorization through payment of the appropriate per-copy fee to the Copyright Clearance Center, Inc., 222 Rosewood Drive, Danvers, MA 01923, (978) 750-8400, fax (978) 750-4470, or on the web at Requests to the Publisher for permission should be addressed to the Permissions Department, John Wiley & Sons, Inc., 111 River Street, Hoboken, NJ 07030, (201) 748-6011, fax (201) 748-6008, or online at. Con A agarose has also be used in other application areas including purification of enzyme-antibody conjugates, purification of IgM and separation of membrane vesicles.PROTEIN PURIFICATION Principles, High Resolution Methods, and Applications Third EditionĬopyright # 2011 by John Wiley & Sons, Inc. Con A is a tetrameric metalloprotein lectin isolated from Canavalia ensiformis (jack bean). Con A is used for the purification of glycoproteins, polysaccharides and glycolipids as it binds molecules containing α-D-mannopyranosyl, α-D-glucopyranosyl and sterically related residues. Jacalin also binds IgD.Ĭoncanavalin A (Con A) Agarose : Concanavalin A (Con A) Agarose consists of Con A coupled to 6% agarose by the cyanogen bromide method. Applications include isolating IgA from human serum and colostrums, isolating human plasma glycoproteins and histochemistry. Jacalin is a α-D-galactose binding lectin purified from jack-fruit (Artocarpus integrifolia) seeds. Immobilized Jacalin : Jacalin, or Artocarpus integrifolia lectin, is a tetrameric two-chain lectin with a molecular weight of 66kDa. Agarose based affinity chromatography resins with immobilized lectins for the purification of glycoproteins.