Drug – bio-affecting and body treating compositions – Designated organic active ingredient containing – Peptide containing doai
Patent
1996-05-15
2000-02-15
Draper, Garnette D.
Drug, bio-affecting and body treating compositions
Designated organic active ingredient containing
Peptide containing doai
514 8, 514 12, 514909, 530399, 530350, 530351, 530402, 530403, 530404, 530405, 530406, 424 851, 4241931, 4241851, 4241941, 42419511, 4241981, A61K 3822, A61K 3800
Patent
active
06025324&
ABSTRACT:
Polyethylene and polypropylene protein conjugates which modulate body weight of ani is and humans for the treatment, prevention and control obesity and associated diseases or conditions, and the recombinant expression of these biologically active proteins in purified and homogeneous forms.
REFERENCES:
patent: 4179337 (1979-12-01), Davis et al.
patent: 4609546 (1986-09-01), Hiratani et al.
patent: 5559208 (1996-09-01), Basinski et al.
patent: 5563243 (1996-10-01), DiMarchi et al.
patent: 5563244 (1996-10-01), DiMarchi et al.
patent: 5563245 (1996-10-01), DiMarchi et al.
patent: 5567678 (1996-10-01), DiMarchi et al.
patent: 5567803 (1996-10-01), Basinski et al.
patent: 5569743 (1996-10-01), DeMarchi et al.
patent: 5569744 (1996-10-01), Basinski et al.
patent: 5574133 (1996-11-01), DiMarchi et al.
patent: 5580954 (1996-12-01), DiMarchi et al.
patent: 5594104 (1997-01-01), Basinski at al.
Francis, Forms on Growth Factors vol. 3, 1992, p. 4-10.
Yamasaki, et al., Novel Polyethylene Glycol Derivatives for Modification of Proteins, Agric. Biol. Chem. vol. 52, No. 8, pp. 2125-2127 (1988).
Yamasaki, et al., Some Proteins of Ricin D Modified with a Methoxypolyethylene Glycol Derivative, Agric. Biol. Chem. vol. 54, No. 10, pp. 2635-2640 (1990).
Gen Bank Accession No. 18812.
Gen Bank Accession No. 18915.
Gen Bank Accession No. 03288.
Gen Bank Accession No. 23332.
Friedman, J. M. et al., Genomics 11:1054-1062 (1991).
Zhang, Y. et al., Nature 372:425-432 (1994).
Monfardini et al., Biconjugate Chem. 6:62-69 (1995).
Barinaga, Obese Protein Slims Mice, Science, vol. 269, pp. 475-476 (1995).
Considine, et al., Evidence Against Either a Premature Stop Codon or the Absence of Obese Gene mRNA in Human Obestity, J. Clin. Invest., vol. 95, pp. 2986-2988 (1995).
Funahashi, et al., Enhanced Expression of Rat Obese (ob) Gene in Adipose Tissues of Ventromedial Hypothalamus (VMH)-Lesioned Rats, Biochemical and Biophysical Research Communications, vol. 211, No. 2, pp. 469-475 (1995).
Olefsky, Weighing in on the Lean Genes, J. Clin. Invest., vol. 95, pp. 2427-2428 (1995).
De Vos, Induction of ob Gene Expression by Corticosteroids Is Accompanied by Body Weight Loss and Reduced Food Intake, The Journal of Biological Chemistry, vol. 270, No. 27, pp. 15958-15961 (1995).
Halaas, et al., Weight-Reducing Effects of the Plasma Protein Encoded by the obese Gene, Science, vol. 269, pp. 543-546 (1995).
Pelleymounter, et al., Effects of the obese Gene Product on Body Weight Regulation in ob/ob Mice, Science, vol. 269, pp. 540-543 (1995).
Stirling, et al., Identification of Microsatellite Markers Near the Human ob Gene and Linkage Studies in NIDDM-Affected Sib Pairs, Diabetes, vol. 44, pp. 999-1001 (1995).
Frederich, et al., Expression of ob mRNA and its Encoded Protein in Rodents, J. Clin. Invest., vol. 96, pp. 1658-1663 (1995).
MaDougald, et al., Regulated expression of the obese gene product (leptin) in white adipose tissue and 3T3-L1 andipocytes, Proc. Natl. Acad. Sci, vol. 92, pp. 9034-9037 (1995).
Ogawa, et al., Molecular Cloning of Rat Obese cDNA and Augmented Gene Expression in Genetically Obese Zucker Fatty (fa/fa) Rats, J. Clin. Invest, vol. 96, pp. 1647-1652 (1995).
Rentsch, et al., Recombinant OB-Gene Produce Reduces Food Intake in Fasted Mice, Biochemical and Biophysical Research Communications, vol. 214, No. 1, pp. 131-136 (1995).
Trayhurn, et al. Effects of fasting and refeeding on ob gene expression in white adipose tissue of lean and obese (ob/ob) mice, FEBS Letters, vol. 368, pp. 488-490 (1995).
Madej, et al., Threading analysis suggest that the obese gene product may be a helical cytokine, FEBS Letters, vol. 373, pp. 13-18 (1995).
Maffei, et al., Leptin levels in human and rodent: Measurement of plasma and leptin and ob RNA in obese and weight-reduced subjects, Nature Medicine, vol. 1, No. 11, pp. 1155-1161, (1995).
Cusin, et al., A Relationship Leading to Clues to the Understanding of Obesity, Diabetes, vol. 44, pp. 1467-1470 (1995).
Frederich, et al., Leptin levels reflect body lipid content in mice: Evidence for diet-induced resistance to leptin action, Nature Medicine, vol. 1, No. 12, pp. 1311-1314 (1995).
He, et al., Genomic Organization, Promoter Activity, and Activation by CCAAT/Enhancer-Binding Protein .alpha., The Journal of Biological Chemistry, vol. 270, No. 48, pp. 28887-28891 (1995).
Maffei, et al., Increased expression in adipocytes of ob RNA in mice with lesions of the hypothalamus and with mutations at the db locus, Proc. Natl. Acad. Sci., vol. 92, pp. 6957-6960 (1995).
Moinat, et al., Modulation of obese gene expression in rat brown and white adipsose tissues, FEBS Letters, vol. 373, pp. 131-134 (1995).
Murakami, et al., Dexamethasone Regulates Obese Expression in Isolated Rat Adipocytes, vol. 214, No. 3, pp. 1260-1267 (1995).
Isse, Structural Organization and Chromosomal Assignment of the Human Obese Gene, The Journal of Biological Chemistry, vol. 270, No. 46, pp. 27728-27733 (1995).
Weigle, et al., Recombinant ob Protein Reduces Feeding and Body Weight in the ob/ob Mouse, J. Clin. Invest., vol. 96, pp. 2065-2070 (1995).
De Sutter, et al., Production of enzymatically active rat protein disulfide isomerase in Escherichia coli, Gene, vol. 141, pp. 163-170 (1994).
Takahara, et al., The ompA Signal Peptide Directed Secretion of Staphylococcal Nuclease A by Escherichia coli, The Journal of Biological Chemistry, vol. 260, No. 5, pp. 2670-2674 (1985).
Groch, et al., Synthesis of the Bacillus subtilis histone-like DNA-binding protein Hbsu in Escherichia coli and secretion into the periplasm,. Gene, vol. 124, pp. 99-103 (1993).
Barone, et al., The Expression in Escherichia coli or Recombinant Human Platelet Factor 4, a Protein with Immunoregulatory Activity, The Journal of Biological Chemistry, vol. 263, No. 18, pp. 8710-8715 (1988).
Hussain, et al., Expression of ricin B chain in Escherichia coli, FEBS Letters, vol. 244, No. 2, pp. 383-387 (1989).
Libby, et al., Expression and Purification of Native Human Granulocyte-Macrophage Colony-Stimulating Factor from an Escherichia coli Secretion Vector, DNA, vol. 6, No. 3, pp. 221-229 (1987).
Monteilhet, et al., Cytoplasmic and periplasmic production of human apolipoprotein E in Escherichia coli using natural and bacterial signal peptides, Gene, vol. 125, pp. 223-228 (1993).
Parker, et al., Overexpression of native human .beta..sub.2 -microglobulin in Escherrichia coli and its purification, Gene, vol. 83, pp. 117-124 (1989).
Le, et al., Purification of Secreted Recombinant Proteins from Escherichia coli, Purification and Analysis of Recombinant Proteins, Seetharam, et al., eds., Ch. 7, pp. 163-181 (in Dekker 1991).
Ghrayeb, et al., Secretion cloning vectors in Escherichia coli, The Embo Journal, vol. 3, No. 10, pp. 2437-2442 (1984).
Barthelemy, et al., Production and secretion of human interleukin 6 into the periplasm of Escherichia coli: efficient processing of N-terminal variants of hIL6 by the E. coli signal peptidase, Journal of Biotechnology, vol. 27, pp. 307-316 (1993).
Fischer, et al., Physiological consequence of expression of soluble and active hen egg white lysozyme in Escherichia coli, Applied Microbiol Biotechnol, vol. 39, pp. 537-540 (1993).
Cheah, et al., Secretion of eukaryotic growth hormones in Escherichia coli is influenced by the sequence of the mature proteins, Gene, vol. 138, pp. 9-15 (1994).
Becker, et al., Expression, secretion and folding of human growth hormone in Escherichia coli, FEBS Letters, vol. 204, No. 1, pp. 145-150 (1986).
Hsiung, et al., High Level Expression, Efficient Secretion and Folding of Human Growth Hormone in Escherichia coli, Biotechnology, vol. 4, pp. 991-995 (1986).
Fraipont, et al., Engineering and overexpression of periplasmic forms of the penicillin-binding protein 3 of Escherichia coli, Biochem. J., vol. 298, pp. 189-195 (1994).
Stanbury, Principles of Fermentation Technology, pp. 212-215 (1984).
Lehninger, Principles of Biochemistry, pp. 128, 145, 109, 131 (Worth 1982).
Zubay, Biochemistry, pp. 47-48, 54-56, 60-61 and 590 (Addison-Wesley 1983).
Stryer, Biochemistry, 2d ed., pp. 19, 20 and 92 (Free
Bailon Pascal Sebastian
Campfield Arthur
Devos Rene
Guisez Yves
Draper Garnette D.
Epstein William H.
Hoffmann-La Roche Inc.
Johnson George W.
Kreisler Lewis J.
LandOfFree
Pegylated obese (ob) protein compositions does not yet have a rating. At this time, there are no reviews or comments for this patent.
If you have personal experience with Pegylated obese (ob) protein compositions, we encourage you to share that experience with our LandOfFree.com community. Your opinion is very important and Pegylated obese (ob) protein compositions will most certainly appreciate the feedback.
Profile ID: LFUS-PAI-O-1905917