Methods for the production of proteins with a desired function

Chemistry: molecular biology and microbiology – Micro-organism – tissue cell culture or enzyme using process... – Recombinant dna technique included in method of making a...

Patent

Rate now

  [ 0.00 ] – not rated yet Voters 0   Comments 0

Details

4351723, 5303871, 53038824, A61K 39395

Patent

active

056270526

ABSTRACT:
The present invention provides a method for producing proteins with a desired function, generally comprising the steps of (a) providing a population of antibody-forming cells suspected of containing at least one cell capable of producing an antibody exhibiting a desired function; (b) suspending the population of antibody-forming cells in a medium, the medium having an indicator system incorporated therein, the indicator system also being capable of indicating the presence and location of a cell which forms antibodies exhibiting the desired function; (c) identifying a cell forming an antibody exhibiting the desired function; (d) isolating the identified antibody-forming cell from the medium; (e) determining the amino acid sequence of the variable region or a portion thereof which coffers the desired function of the antibody produced by the isolated antibody-forming cell; and (f) synthesizing a protein with a desired function, the protein containing the amino acid sequence of the variable region or portion thereof which confers the desired function.

REFERENCES:
patent: 4035316 (1977-07-01), Yen et al.
patent: 4138383 (1979-02-01), Rembaum et al.
patent: 4143203 (1979-03-01), Rigopulos et al.
patent: 4157323 (1979-06-01), Yen et al.
patent: 4230685 (1980-10-01), Senyei et al.
patent: 4357142 (1982-11-01), Schall, Jr. et al.
patent: 4363634 (1982-12-01), Schall, Jr.
patent: 4452773 (1984-06-01), Molday
patent: 4550075 (1985-10-01), Bacquet et al.
patent: 4618577 (1986-10-01), Handley et al.
patent: 4689310 (1987-08-01), Kramer et al.
Zhang et al. Hum. Antibiod. Hybridomas 1990 1(1) 42-46.
Huse et al., "Generation of a Large Combinatorial Library of the Immunoglobulin Repertoire in Phage Lambda," Science 246:1275-1281, 1989.
Lazar et al., "Transforming Growth Factor .alpha.: Mutation of Aspartic Acid 47 and Leucine 48 Results in Different Biological Activities," Molecular and Cellular Biology 8(3): 1247-1252, 1988.
Burgess et al., "Possible Dissociation of the Heparin-Binding and Mitogenic Activities of Heparin-Binding (Acidic Fibroblast) Growth Factor-1 from Its Receptor-Binding Activities by Site-Directed Mutagenesis of a Single Lysine Residue," Journal of Cell Biology 111: 2129-2138, 1990.
Goding, J., in Monoclonal Antibodies: Principles and Practice, 2nd Ed., 1986, pp. 76-89.
Sahagan et al., "A Genetically Engineered Murine/Human Chimeric Antibody Retains Specificity for Human Tumor-Associated Antigen," Journal of Immunology 137(3): 1066-1074, 1986.
Orlandi et al., "Cloning Immunoglobulin Variable Domains for Expression by the Polymerase Chain Reaction," Proc. Natl. Acad. Sci. USA 86: 3833-3837, 1989.
Liu et al., "Chimeric Mouse-Human IgG1 Antibody That Can Mediate Lysis of Cancer Cells," Proc. Natl. Acad. Sci. USA 84: 3439-3443, 1987.
Kanagawa, O., "Antibody-Mediated Activation of T Cell Clones as a Method for Screening Hybridomas Producing Antibodies to the T Cell Receptor," Journal of Immunological Methods 110: 169-178, 1988.
Allen, P., "Construction of Murine T-T-Cell Hybridomas," in Monoclonal Antibody Production Techniques and Applications, L.B. Schook ed., Marcel Dekker, Inc. New York, 1987, pp. 25-35.
Aggarwal and Bringman, "Production and Purification of Lymphokines and Their Monoclonal Antibodies" in Monoclonal Antibody Production Techniques and Applications, L.B. Schook ed., Marcel Dekker, Inc. New York, 1987, pp. 173-187.
Kingsman and Kingsman, "Biotechnology," in Genetic Engineering: An Introduction to Gene Analysis and Exploitation in Eukaryotes, Blackwell Scientific Publications, Oxford, 1988, pp. 414-456.
Larrick et al., "Polymerase Chain Reaction Using Mixed Primers: Cloning of Human Monoclonal Antibody Variable Region Genes from Single Hybridoma Cells," Bio/Technology 7: 934-938, 1989.
Huston et al., "Protein Engineering of Antibody Binding Sites: Recovery of Specific Activity in an Anti-Digoxin Single-Chain Fv Analogue Produced in Escherichia coli,"Proc Natl. Acad. Sci. USA 85: 5879-5883, 1988.
Riechmann et al., "Reshaping Human Antibodies for Therapy," Nature 332: 323-327, 1988.
Frohman et al., "Rapid Production of Full-Length cDNAs from Rare Transcripts: Amplification Using a Single Gene-Specific Oligonucleotide Primer," Proc. Natl. Acad. Sci. USA 85: 8998-9002, 1988.
Loh et al., "Polymerase Chain Reaction with Single-Sided Specificity: Analysis of T Cell Receptor .sigma. Chain," Science 243: 217-220, 1989.
Samoilovich et al., "Hybridoma Technology: New Developments of Practical Interest," Journal of Immunological Methods 101: 153-170, 1987.
Price, P., "Hybridoma Technology," Advances in Cell Culture 4: 157-177, 1985.
Bayer and Wilchek, "The Avidin-Biotin Complex as a Tool in Molecular Biology," TIBS 3(11) N257-N259, 1978.
Wilchek and Bayer, "The Avidin-Biotin Complex in Bioanalytical Applications," Analytical Biochemistry 171:1-32, 1988.
Bayer and Wilchek, "The Use of the Avidin-Biotin Complex as a Tool in Molecular Biology," Methods of Biochemical Analysis:1-45, 1980.

LandOfFree

Say what you really think

Search LandOfFree.com for the USA inventors and patents. Rate them and share your experience with other people.

Rating

Methods for the production of proteins with a desired function does not yet have a rating. At this time, there are no reviews or comments for this patent.

If you have personal experience with Methods for the production of proteins with a desired function, we encourage you to share that experience with our LandOfFree.com community. Your opinion is very important and Methods for the production of proteins with a desired function will most certainly appreciate the feedback.

Rate now

     

Profile ID: LFUS-PAI-O-2131917

  Search
All data on this website is collected from public sources. Our data reflects the most accurate information available at the time of publication.