Applications of Enzyme Biotechnology PDF
Preview Applications of Enzyme Biotechnology
APPLICATIONS OF ENZYME BIOTECHNOLOGY INDUSTRY -UNIVERSITY COOPERATIVE CHEMISTRY PROGRAM SYMPOSIA Published by Texas A&M University Press ORGANOMETALLIC COMPOUNDS Edited by Bernard L. Shapiro HETEROGENEOUS CAT AL YSIS Edited by Bernard L. Shapiro NEW DIRECTIONS IN CHEMICAL ANALYSIS Edited by Bernard L. Shapiro APPLICATIONS OF ENZYME BIOTECHNOLOGY Edited by Jeffery W. Kelly and Thomas O. Baldwin CHEMICAL ASPECTS OF ENZYME BIOTECHNOLOGY: Fundamentals Edited by Thomas O. Baldwin, Frank M. Raushel, and A. Ian Scott DESIGN OF NEW MATERIALS Edited by D. L. Cocke and A. Clearfield FUNCTIONAL POLYMERS Edited by David E. Bergbreiter and Charles R. Martin METAL-METAL BONDS AND CLUSTERS IN CHEMISTRY AND CAT AL YSIS Edited by John P. Fackler, Jr. OXYGEN COMPLEXES AND OXYGEN ACTIVATION BY TRANSITION METALS Edited by Arthur E. Martell and Donald T. Sawyer APPLICATIONS OF ENZYME BIOTECHNOLOGY Edited by Jeffery W. Kelly and Thomas O. Baldwin Texas A&M University College Station, Texas Springer Science+Business Media, LLC Library of Congress Catalog1ng-in-PublIcat1on Data Texas A & M University, IUCCP Symposium on Applications of Enzyme Biotechnology (9th : 199Ό Applications of enzyme biotechnology / edited by Jeffery W. Kelly and Thomas 0. Baldwin. p. cm. — (Industry-university cooperative chemistry program sympos i a ) "Proceedings of the Texas A & M University, IUCCP Ninth Annual Symposium on Applications of Enzyme Biotechnology, held March 18-21, 1991, in College Station, Texas"—T.p. verso. Includes bibliographical references and index. 1. Enzymes—Biotechnology—Congresses. I. Kelly, Jeffery W. II. Baldwin, Thomas 0. III. Title. IV. Series. TP248.65.E59T47 1991 660' .634—dc20 91-41625 . CIP Proceedings of the Texas A&M University, IUCCP Ninth Annual Symposium on Applications of Enzyme Biotechnology, held March 18-21, 1991, in College Station, Texas ISBN 978-1-4757-9237-9 ISBN 978-1-4757-9235-5 (eBook) DOI 10.1007/978-1-4757-9235-5 © 1991 Springer Science+Business Media New York Originally published by Plenum Press, New York in 1991 Softcover reprint of the hardcover 1st edition 1991 All rights reserved No part of this book may be reproduced, stored in a retrieval system, o r transmitted in any form or by any means, electronic, mechanical, photocopying, microfilming, recording, or otherwise, without written permission from the Publisher FOREWORD The Industry-University Cooperative Chemistry Program (IUCCP) has sponsored eight previous international symposia covering a range of topics of interest to industrial and academic chemists. The ninth IUCCP Symposium, held March 18-21, 1991 at Texas A&M University was the second in a two part series focusing on Biotechnology. The title for this Symposium "Applications of Enzyme Biotechnology" was by design a rather all encompassing title, similar in some respects to the discipline. Biotechnology refers to the application of biochemistry for the development of a commercial product. Persons employed in or interested in biotechnology may be chemists, molecular biologists, biophysicists, or physicians. The breadth of biotech research projects requires close collaboration between scientists of a variety of backgrounds, prejudices, and interests. Biotechnology is a comparatively new discipline closely tied to new developments in the fields of chemistry, biochemistry, molecular biology and medicine. The primary function of Texas A&M University is to educate students who will be appropriately trained to carry out the mission of biotechnology. The IUCCP Symposium serves as an important forum for fostering closer ties between academia and industry and exchanging ideas so important to this evolving area. The topics that were discussed during this conference, include the oxidation of alkanes by enzymes, protein folding, waste remediation, protein purification techniques, and protein expression systems. These titles represent a smorgasbord of topics of importance to the biotechnology industry. The manuscripts submitted point out not only the tremendous progress made in each one of those areas, but also discuss the challenges still facing the industry as a whole. Many of the problems facing the biotech companies are the same problems that academic biochemists and molecular biologists face on a daily basis. It was clear to all participants that general solutions to thorny problems such as protein expression, waste remediation, and refolding recombinant proteins could form the basis for very successful companies. This pioneering and entrepreneurial spirit is what makes biotechnology so exciting and what attracts some of the brightest people to this area. We are deeply indebted to the IUCCP sponsoring companies Abbott Labs, Hoechst-Celanese, Monsanto Chemical Company, BF Goodrich, Dow Chemical Company for providing the necessary resources to carry out this endeavor. v The co-chainnen of the conference were Professor Thomas O. Baldwin, and Frank M. Raushel of the Texas A&M University Chemistry Department. The program was developed by an academic steering committee consisting of the co-chainnen and members appointed by the sponsoring chemical companies Dr. James Burrington, BP America; Dr. Robert Durrwater, Hoechst-Celanese; Dr. Barry Haymore, Monsanto Chemical Company; Dr. Mehmet Gencer, BF Goodrich; Dr. Paul Swanson, Dow Chemical Company; and Professor Arthur Martell, Texas A&M IUCCP Coordinator. In closing, the organizers of the Ninth IUCCP Symposium must recognize the contributions that have been made to the symposium by Mrs. Mary Martell, who dealt with the innumerable details necessary for a successful symposium. Her pleasant nature and efficiency are appreciated. Finally, we wish to thank the Texas A&M graduate students who donated their time to ensure smooth operations. Thomas O. Baldwin Jeffery W. Kelly vi CONTENTS Minisymposium on Diagnostic Therapeutic Applications of Radiolabeled Antibodies Radiolabeled Antibodies: Introduction and Metal Conjugation Techniques .. . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . .. 1 Sally W. Schwarz and Michael J. Welch Methods for the Radiohalogenation of Antibodies ........................ 15 Michael R. Zalutsky, Pradeep K. Garg, Ganesan Vaidyanathan, and Sudha Garg Diagnosis and Therapy of Brain Tumors Utilizing Radiolabeled Monoclonal Antibodies ............................................. 29 Herbert E. Fuchs, Michael R. Zalutsky, Gary E. Archer, and Darell D. Bigner Selective Functionalization of Alkanes by Enzymes and Their Models Oxygenation by Methane Monooxygenase: Oxygen Activation and Component Interactions . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . .. 39 Wayne A. Froland, Kristoffer K. Andersson, Sang-Kyu Lee, Yi Liu, and John D. Lipscomb Structure and Mechanism of Action of the Enzyme(s) Involved in Methane Oxidation ............................................... 55 Howard Dalton Studies of Methane Monooxygenase and Alkane Oxidation Model Complexes 69 Amy C. Rosenzweig, Xudong Feng, and Stephen J. Lippard Relevance of Gif Chemistry to Enzyme Mechanisms 87 Derek H.R. Barton and Dario Doller Protein Folding and Refolding for Commercially Important Proteins Transthyretin Acid Induced Denaturation Is Required for Amyloid Fibril Formation in Vitro . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . .. 99 Wilfredo Colon and Jeffery W. Kelly Isolation and Characterization of Natural and Recombinant Cyclophilins 109 T.F. Holzman, S.W. Fesik, C. Park, and J.L. Kofron Mutations Affecting Protein Folding and Misfolding in Vivo . . . . . . . . . . . . . . .. 129 Anna Mitraki, Ben Fane, Cameron Haase-Pettingell, and Jonathan King Protein Folding: Local Structures, Domains, and Assemblies . . . . . . . . . . . . . . .. 137 Rainer Jaenicke VII Environmental Biotechnology Applications of Controlled Pore Inert Materials as Immobilizing Surfaces for Microbial Consortia in Wastewater Treatment ................. 153 Ralph J. Portier Organophosphorus Cholinesterase Inhibitors: Detoxification by Microbial Enzymes . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . .. 165 Joseph J. DeFrank Applications of Molecular Biology Techniques to the Remediation of Hazardous Waste . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . " 181 Burt D. Ensley Dehalogenation of Organohalide Pollutants by Bacterial Enzymes and Coenzymes 191 Lawrence P. Wackett Protein Processing-New Techniques Immobilized Artificial Membrane Chromatography: Surface Chemistry and Applications ........................................ 201 Charles Pidgeon, Craig Marcus, and Francisco Alvarez Perfusion Chromatography: Recent Developments and Applications . . . . . . . . . .. 221 Noubar B. Afeyan, Scott P. Fulton, and Fred E. Regnier High Performance Capillary Electrophoresis of Proteins and Peptides: A Minireview .......................................... 233 Robert S. Rush Genetic Alterations Which Facilitate Protein Purification: Applications in the Biopharmaceutical Industry ............................ 251 Helmut M. Sassenfeld, Michael Deeley, John Rubero, Janet C. Shriner, and Hassan Madani Expression Systems-Exogenous Proteins Bacillus subtilis: A Model System for Heterologous Gene Expression 261 Roy H. Doi, Xiao-Song He, Paula McCready, and Nouna Bakheit Aspergillus niger var. awamori as a Host for the Expression of Heterologous Genes . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . .. 273 Randy M. Berka, Frank T. Bayliss, Peggy Bloebaum, Daniel Cullen, Nigel S. Dunn-Coleman, Katherine H. Kodama, Kirk J. Hayenga, Ronald A. Hitzeman, Michael H. Lamsa, Melinda M. Przetak, Michael W. Rey, Lori J. Wilson, and Michael Ward Poxvirus Vectors: Mammalian Cytoplasmic-Based Expression Systems 293 Bernard Moss Appendix . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . .. 301 Index. . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . .. 303 viii RADIOLABELED ANTIBODIES: INTRODUCTION AND METAL CONJUGATION TECHNIQUES Sally W. Schwarz and Michael J. Welch Mallinckrodt Institute of Radiology Washington University, 510 S. Kingshighway St. Louis, MO, U.S.A. INTRODUCTION The use of radiolabeled antibodies in the detection and treatment of cancer has been in practice since the early 1980's. Radioimmunoimaging is an in vivo diagnostic technique where a radiolabeled antibody is taken up or bound to an antigen in a target tissue. This allows for non-invasive imaging of the antigen containing tissue, using a gamma camera or a positron emission tomograph (PET) scanner, for subsequent therapy or resection of the tissue if necessary. Radioimmunotherapy is the delivery of a therapeutic quantity of a radioisotope to the same antigen containing tissue to ablate or reduce a primary or metastatic carcinoma. This chapter will cover the basic principles of antibodies, subsequent conjugation with bifunctional chelates and radiolabeling for the purpose of radioimmunoimaging or radioimmunotherapy. Antibodies (Ab) are immunoglobulins produced as a result of the body's immune response. This reaction is triggered when the body is faced with foreign matter. "Immunogens" or antigens can be bacteria, viruses, fungi, or any foreign proteins. Each antigen (Ag) has more than one epitope or antigenic determinant (figure 1). These epitopes represent only a small fraction of the Ag molecule. Once a single Ag is injected into the bloodstream it interacts either by direct associaton with a B-Iymphocyte or the Ag is "processed" by macrophages and "presented" to the B lymphocyte by a T-helper cell. After interaction with the B-Iymphocyte the B-cell is activated, and proliferates. It then differentiates into a plasma cell which secretes the Ah specific for the Ag (figure 2). After Ag injection there is a lag time of approximately one week before production of these Ag specific Ab. Antibodies are glycoproteins consisting of five different classes: IgG, IgM, IgA, IgE and IgD (figure 3). Each group contains one or more subunits of a Y shape. Each Y unit contains 4 polypeptides, two identical segments called heavy chains and 2 segments called light chains (figure 4). Each class of Ab has a specific type of heavy chain, but there are only 2 types of light chain polypeptides known as kappa (lC) and lambda ().). These chains are held together with multiple inter and intra disulfide bonds and non-covalent bonds. When the body is faced with an unknown Ag, the IgM class of immunoglobulins is
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