Biotinylation of proteins

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

435 697, 435440, 435471, 4353201, 536 231, 536 234, C12N 1509, C12N 1511, C12N 1563, C12N 1570

Patent

active

058742395

DESCRIPTION:

BRIEF SUMMARY
BACKGROUND OF THE INVENTION

1. Field of the Invention
The present invention relates to methods for producing biotinylated proteins in vitro and in recombinant host cells. The invention therefore relates to the field of molecular biology, but given the diverse uses for recombinant proteins, the invention also relates to the fields of chemistry, pharmacology, biotechnology, and medical diagnostics.
2. Description of the Background Art
The ability to synthesize DNA chemically has made possible the construction of peptides and proteins not otherwise found in nature and useful in a wide variety of methods that would otherwise be very difficult or impossible to perform. One illustrative example of this technology relates to the class of molecules known as receptors. Receptor proteins mediate important biological functions through interactions with ligands. For many years, researchers have attempted to isolate and identify ligands that interact with receptors in ways that can help ameliorate human (and other) disease. The advent of molecular biology has revolutionized the way these researchers study receptor-ligand interaction. For instance, standard molecular biology techniques have enabled the cloning and high-level expression of many receptors in recombinant host cells.
The patent literature, for instance, is replete with publications describing the recombinant expression of receptor proteins. See, e.g., PCT Patent Pub. No. 91/18982 and U.S. Pat. Nos. 5,081,228 and 4,968,607, which describe recombinant DNA molecules encoding the IL-1 receptor; U.S. Pat. Nos. 4,816,565; 4,578,335; and 4,845,198, which describe recombinant DNA and proteins relating to the IL-2 receptor; PCT Patent Pub. No. 91/08214, which describes EGF receptor gene related nucleic acids; PCT Patent Pub. No. 91/16431 and U.S. Pat. No. 4,897,264, which describe the interferon gamma receptor and related proteins and nucleic acids; European Patent Office (EPO) Pub. No. 377,489, which describes the C5a receptor protein; PCT Patent Pub. No. 90/08822, which describes the EPO receptor and related nucleic acids; and PCT Patent Pub. No. 92/01715, which describes MHC receptors.
Several of the above publications not only describe how to isolate a particular receptor protein (or the gene encoding the protein) but also describe variants of the receptor that may be useful in ways the natural or native receptor is not. For instance, PCT Patent Pub. No. 91/16431 describes soluble versions of the gamma interferon receptor, while PCT Patent Pub. No. 92/01715 describes how to produce soluble cell-surface dimeric proteins. This latter technology involves expression of the receptor with a signal for lipid attachment; once the lipid is attached to the receptor, the receptor becomes anchored in the cell membrane, where the dimeric form of the receptor is assembled. See also U.S. Ser. No. 947,339, filed on Sep. 18, 1992, and incorporated herein by reference for all purposes, which describes how HPAP-containing receptors can be cleaved from the cell surface and how the anchoring sequences that remain can serve as recognition sequences for antibodies that are used to immobilize the receptor.
The advances made with respect to receptor cloning and expression have been accompanied by advances in technology relating to methods for screening a receptor against compounds that may interact with the receptor in a desired fashion. One such advance relates to the generation of large numbers of compounds, or potential ligands, in a variety of random and semi-random "peptide diversity" generation systems. These systems include the "peptides on plasmids" system described in U.S. patent application Ser. No. 963,321, filed Oct. 15, 1992, which is a continuation-in-part of U.S. patent application Ser. No. 778,233, filed Oct. 16, 1991; the "peptides on phage" system described in U.S. patent application Ser. No. 718,577, filed Jun. 20, 1991, which is a continuation-in-part of Ser. No. 541,108, filed Jun. 20, 1990; Cwirla et al., August 1990, Proc. Natl. Acad. Sci. USA 87: 6378-6382; Barr

REFERENCES:
patent: 5723584 (1998-03-01), Schatz
Anton et al. (1991), "Development of biotinylated analog of substance P for use as a receptor probe," Chemical Abstracts, vol. 115, No. 21, p. 110, abstract No. 223703.
Anton et al. (1991), "Biotinylation of a bombesin/gastrin-releasing peptide analog for use as a receptor probe," Chemial Abstracts, vol. 115, No. 1, p. 135, abstract No. 1318.
Yamamo et al. (1992), "In vivo biotinylation of fusion proteins expressed in escherichia coli with a sequence of propionibacterium freudenreichii transcarboxylase 1.3S biotin subunit," Biosci. Biotechnol. Biochem 56(7):1017-1026.
Buoncristiani et al. (1988), J. Biol. Chem. 263(2):1013-1016, "Overproduction and rapid purification of the biotin operon repressor for E. coli".
Cress et al. (1993), Promega Notes 42: 2-7, "Purification: A one-step nondenaturing purification method for recombinant proteins produced in E. coli".
Cronan (1989), Cell 58:427-429, "The E. coli bio operon: transcriptional repression by an essential protein modification enzyme".
Cronan (1990), J. Biol. Chem. 265(18):10327-10333, "Biotination of Proteins in Vivo".
Freytag and Collier (1984), J. Biol. Chem. 259:12831-12837, "Molecular cloning of a cDNA for human pyruvate carboxylase".
Lamhonwah et al. (1987), Archives of Biochem. & Biophysics, 254: 631-636, "Sequence homology around the biotin-binding site of human propionyl-CoA carboxylase and pyruvate carboxylase".
Murtif et al. (1985), Proc. Natl. Acad. Sci. USA 82:5617-5621, "Cloning and expression of the 1.3S biotin-containing subunit of transcarboxylase".
Murtif et al. (1987), J. Biol. Chem. 262(24):11813-11816, "Mutagenesis affecting the carboxyl terminus of the biotinyl subunit of transcarboxylase".
Reed and Cronan (1991), J. Biol Chem. 266:11425-11428, "Escherichia coli exports previously folded and biotinated protein domains".
Schatz, (1993), Bio/Technology, 11:1138-1143, "Use of peptide libraries to map the substrate specificity of a peptide-modifying enzyme: A 13 residue consensus peptide specifies biotinylation in escherichia coli".
Shenoy et al. (1988), FASEB J. 2(9);2505-2511, "Effect of mutations at Met-88 and Met-90 on the biotination of Lys-89 of the apo 1.3S subunit of transcarboxylase".
Shenoy et al. (1992), J. Biol. Chem. 267(26):18407-18412, "The importance of methionine residues for the catalysis of the biotin enzyme, transcarboxylase".
Thampy et al. (1988), Archives of Biochem. & Biophysics, 266: 270-276, "A rapid purification method for rat liver pyruvate carboxylase and amino acid sequence analysis of NH.sub.2 -terminal and biotin peptide".

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

Biotinylation of proteins does not yet have a rating. At this time, there are no reviews or comments for this patent.

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

Rate now

     

Profile ID: LFUS-PAI-O-305622

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