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  • 1
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    Generation of a large combinatorial library of the immunoglobulin repertoire in phage lambda (1989)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1989-12-08
    Description: A novel bacteriophage lambda vector system was used to express in Escherichia coli a combinatorial library of Fab fragments of the mouse antibody repertoire. The system allows rapid and easy identification of monoclonal Fab fragments in a form suitable for genetic manipulation. It was possible to generate, in 2 weeks, large numbers of monoclonal Fab fragments against a transition state analog hapten. The methods described may supersede present-day hybridoma technology and facilitate the production of catalytic and other antibodies.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Huse, W D -- Sastry, L -- Iverson, S A -- Kang, A S -- Alting-Mees, M -- Burton, D R -- Benkovic, S J -- Lerner, R A -- New York, N.Y. -- Science. 1989 Dec 8;246(4935):1275-81.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Molecular Biology, Research Institute of Scripps Clinic, La Jolla, CA 92037.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2531466" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Antibodies, Monoclonal/*biosynthesis/genetics ; Antibody Specificity ; Antigen-Antibody Reactions ; Bacteriophage lambda/*genetics ; Base Sequence ; Cloning, Molecular/methods ; Escherichia coli/genetics ; Gene Amplification ; Gene Library ; *Genetic Vectors ; Hemocyanin/analogs & derivatives/immunology ; Immunoglobulin Fab Fragments/biosynthesis ; Immunoglobulin Fragments/*biosynthesis/genetics ; Mice ; Molecular Sequence Data ; Organophosphorus Compounds/immunology ; Recombinant Proteins/biosynthesis/genetics
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
    Published by American Association for the Advancement of Science (AAAS)
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  • 2
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    Catalytic antibodies with lipase activity and R or S substrate selectivity (1989)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1989-04-28
    Description: The specific hydrolysis of unactivated esters bearing an R or S enantiomeric alcohol has been achieved by two separate classes of catalytic antibodies induced to bind either the R or S substrates. The antibodies exhibit rate accelerations (10(3) to 10(5] above background hydrolysis that, coupled with their antipodal specificity, provide a novel set of reagents for use in synthesis.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Janda, K D -- Benkovic, S J -- Lerner, R A -- New York, N.Y. -- Science. 1989 Apr 28;244(4903):437-40.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Molecular Biology, Research Institute of Scripps Clinic, La Jolla, CA 92037.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2717936" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; *Antibodies, Monoclonal/immunology ; Antibody Specificity ; Antigens/immunology ; Benzyl Alcohols/metabolism ; *Catalysis ; Esters/metabolism ; Haptens ; Hemocyanin/immunology ; Hydrolysis ; Immunization ; Kinetics ; Lipase/*metabolism ; Mice ; Mice, Inbred A ; Molecular Structure ; Organophosphonates/immunology ; Stereoisomerism ; Substrate Specificity
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 3
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    An unexpectedly efficient catalytic antibody operating by ping-pong and induced fit mechanisms (1991)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1991-05-03
    Description: A transition state analogue was used to produce a mouse antibody that catalyzes transesterification in water. The antibody behaves as a highly efficient catalyst with a covalent intermediate and the characteristic of induced fit. While some features of the catalytic pathway were programmed when the hapten was designed and reflect favorable substrate-antibody interactions, other features are a manifestation of the chemical potential of antibody diversity. The fact that antibodies recapitulate mechanisms and pathways previously thought to be a characteristic of highly evolved enzymes suggests that once an appropriate binding cavity is achieved, reaction pathways commensurate with the intrinsic chemical potential of proteins ensue.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Wirsching, P -- Ashley, J A -- Benkovic, S J -- Janda, K D -- Lerner, R A -- GM43858-01/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1991 May 3;252(5006):680-5.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Chemistry, Scripps Research Institute, La Jolla, CA 92037.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2024120" target="_blank"〉PubMed〈/a〉
    Keywords: Acylation ; Alcohols/metabolism ; Animals ; Antibodies, Monoclonal/immunology/*metabolism ; Antibody Specificity ; Binding Sites, Antibody ; *Catalysis ; Enzymes/metabolism ; Esterification ; Haptens ; Kinetics ; Mice ; Water
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
    Published by American Association for the Advancement of Science (AAAS)
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  • 4
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    At the crossroads of chemistry and immunology: catalytic antibodies (1991)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1991-05-03
    Description: Immunochemistry has historically focused on the nature of antigenicity and antibody-antigen recognition. However, in the last 5 years, the field of immunochemistry has taken a new direction. With the aid of mechanistic and synthetic chemistry, the vast network of molecules and cells of the immune system has been tapped to produce antibodies with a new function--catalytic antibodies. Because antibodies can be generated that selectively bind almost any molecule of interest, this new technology offers the potential to tailor-make highly selective catalysts for applications in biology, chemistry, and medicine. In addition, catalytic antibodies provide fundamental insight into important aspects of biological catalysis, including the importance of transition-state stabilization, proximity effects, general acid and base catalysts, electrophilic and nucleophilic catalysis, and strain.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Lerner, R A -- Benkovic, S J -- Schultz, P G -- New York, N.Y. -- Science. 1991 May 3;252(5006):659-67.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Chemistry, Scripps Research Institute, La Jolla, CA 92037.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2024118" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; *Antibodies/chemistry/immunology/metabolism ; Antibodies, Monoclonal/immunology/metabolism ; Antibody Specificity ; Antigens/chemistry/immunology/metabolism ; Binding Sites, Antibody ; *Catalysis ; Chemical Phenomena ; Chemistry ; Haptens ; Hydrogen-Ion Concentration ; Hydrolysis ; Metals ; Molecular Conformation ; Recombinant Proteins ; Thermodynamics ; Zinc
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 5
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    Efficient aldolase catalytic antibodies that use the enamine mechanism of natural enzymes (1995)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1995-12-15
    Description: Antibodies that catalyze the aldol reaction, a basic carbon-carbon bond-forming reaction, have been generated. The mechanism for antibody catalysis of this reaction mimics that used by natural class I aldolase enzymes. Immunization with a reactive compound covalently trapped a Lys residue in the binding pocket of the antibody by formation of a stable vinylogous amide. The reaction mechanism for the formation of the covalent antibody-hapten complex was recruited to catalyze the aldol reaction. The antibodies use the epsilon-amino group of Lys to form an enamine with ketone substrates and use this enamine as a nascent carbon nucleophile to attack the second substrate, an aldehyde, to form a new carbon-carbon bond. The antibodies control the diastereofacial selectivity of the reaction in both Cram-Felkin and anti-Cram-Felkin directions.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Wagner, J -- Lerner, R A -- Barbas, C F 3rd -- CA27489/CA/NCI NIH HHS/ -- New York, N.Y. -- Science. 1995 Dec 15;270(5243):1797-800.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Chemistry, Scripps Research Institute, La Jolla, CA 92037, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8525368" target="_blank"〉PubMed〈/a〉
    Keywords: Acetone/chemistry ; Aldehydes/chemistry ; Animals ; Antibodies, Catalytic/biosynthesis/*chemistry/immunology ; Antibodies, Monoclonal/chemistry/immunology ; Antibody Specificity ; Catalysis ; Fructose-Bisphosphate Aldolase/*chemistry/immunology ; Haptens/chemistry/immunology ; Lysine/chemistry ; Mice ; Substrate Specificity
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 6
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    Induction of an antibody that catalyzes the hydrolysis of an amide bond (1988)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1988-09-02
    Description: Catalysis of amide bond hydrolysis is of singular importance in enzymology. An antibody was induced to an analog of a high-energy intermediate anticipated along the reaction coordinate of amide hydrolysis. This antibody is an amidase with high specificity and a large rate enhancement (250,000) relative to the uncatalyzed reaction. This reaction represents the kinetically most difficult hydrolysis reaction yet catalyzed by an antibody.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Janda, K D -- Schloeder, D -- Benkovic, S J -- Lerner, R A -- New York, N.Y. -- Science. 1988 Sep 2;241(4870):1188-91.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Molecular Biology, Research Institute of Scripps Clinic, La Jolla, CA 92037.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/3413482" target="_blank"〉PubMed〈/a〉
    Keywords: Amidohydrolases/metabolism ; Animals ; Antibodies, Monoclonal/biosynthesis/*physiology ; Antibody Specificity ; Antigens/immunology ; *Catalysis ; Chemical Phenomena ; Chemistry ; Hemocyanin/analogs & derivatives/immunology ; Hydrolysis ; Immunization ; Kinetics ; Mice ; Organophosphorus Compounds/immunology ; Substrate Specificity
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
    Published by American Association for the Advancement of Science (AAAS)
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