Method for sterilizing animals using hormone-toxin conjugate com

Drug – bio-affecting and body treating compositions – Designated organic active ingredient containing – Peptide containing doai

Patent

Rate now

  [ 0.00 ] – not rated yet Voters 0   Comments 0

Details

514 12, 530313, 530328, 530324, 530398, 530345, A61K 3800, C07K 500, C07K 700, C07K 1700

Patent

active

054880360

ABSTRACT:
Certain toxic compounds (T) such as, for example, compounds based upon diphtheria toxin, ricin toxin, pseudomonas exotoxin, .alpha.-amanitin, pokeweed antiviral protein (PAP), ribosome inhibiting proteins, especially the ribosome inhibiting proteins of barley, wheat, corn, rye, gelonin and abrin, as well as certain cytotoxic chemicals such as, for example, melphalan and daunomycin can be conjugated to certain analogs of gonadotropin-releasing hormone to form a class of compounds which, when injected into an animal, destroy the gonadotrophs of the animal's anterior pituitary gland. Hence such compounds may be used to sterilize such animals and/or to treat certain sex hormone related diseases.

REFERENCES:
patent: 4081533 (1978-03-01), Cheesmana
patent: 4201770 (1980-05-01), Stevens
patent: 4302386 (1981-11-01), Stevens
patent: 4400376 (1983-08-01), Sanderson
patent: 4444759 (1984-04-01), Rivier et al.
patent: 4526716 (1985-07-01), Stevens
patent: 4691006 (1987-09-01), Stevens
patent: 4767842 (1988-08-01), Stevens
patent: 4863857 (1989-09-01), Blalock et al.
patent: 5378688 (1995-01-01), Nett et al.
Bacha et al., "Organ-Specific Binding of a Thyrotropin-Releasing Hormone-Diphtheria Toxin Coplex after Intravenous Administration to Rats", pp. 1072-1076, 1983, Endocrinology, vol. 113.
Bacha et al., "Systemic Toxicity of Diphtheria Toxin-Related Fragments (CRM26, CRM45)", a Hormone-Toxin Hybrid Protein (TRH-CRM45), and Ricin A.sup.1 (42234), pp. 131-138, 1986, Proc. Soc. Exp. Biol. Med., vol. 181.
Bacha et al., "Thyrotropin-Releasing Hormone-Diphtheria Toxin-Related Polypeptide Conjugates; Potential Role of the Hydrophobic Domain in Toxin Entry", pp. 1565.1570, 1983, J. Biol. Chem., vol. 258, Feb.
Bourdon et al., "The Potential of Monoclonal Antibodies as Carriers of Radiation and Drugs for mmunodetection and Therapy of Brain Tumors", pp. 79-101, 1984, Prog. exp. Tumor Res., vol. 28.
Cawley et al., "Epidermal Growth Factor-Toxin A Chain Conjugates: EGF-Ricin A is a Potent Toxin While EGF-Diphtheria Fragment A is Nontoxic", pp. 563-570, 1980, Cell, vol. 22, Nov.
Chang te al., "Artificial Hybrid Protein Containing a Toxic Protein Fragment and a Cell Membrane Receptor-Binding Moiety in a Disulfide Conjugate", pp. 1515-1522, 1977, J. Biol. Chem., vol. 252, Feb.
Chaudhary et al., "Activity of a Recombinant Fusion Protein Between Transforming Growth Factor Type .alpha. and Pseudomonas Toxin", pp. 4538-4542, 1987, Proc. Natl. Acad. Sci. USA, vol. 84, Jul.
Colombatti et al., "Cloned Fragment of Diphtheria Toxin Linked to T Cell-Specific Antibody Identifies Regions of B Chain Active in Cell Entry", pp. 3030-3035, 1986, J. Biol. Chem., vol. 261, Mar.
Greenfield et al., "Mutations in Diphtheria Toxin Separate Binding from Entry and Amplify Immunotoxin Selectivity", pp. 536-539, 1987, Science, vol. 238, Oct.
Meyers et al., "Specific Chemical Cleavage of Diphtheria Toxin With Hydroxylamine", pp. 17122-17127, 1988, J. Biol. Chem., vol. 263, No. 32, Nov.
Murphy et al., "Genetic Construction Expression, and Melanoma-Selective Cytotoxicity of a Diphtheria Toxin-Related .alpha.-Melanocyte-Stimulating Hormone Fusion Protein", pp. 8258-8262, Proc. Natl. Acad. Sci. USA, vol. 83, Nov.
Myers, "Hybrid Toxins: an Approach to Cell Specific Toxicity", 1987, Dissertation submitted to the Division of Animal Science and the Graduate School of the University of Wyoming, Laramie, Wyoming.
Myers, D. A., et al., "Protein-Peptide Conjugation By A Two-Phase Reaction", p. 343, 1985, Biochem J., 227:1.
Oeltmann et al., "A Hybrid Protein Containing the Toxic Subunit of Ricin and the Cell-Specific Subunit of Human Chorionic Gonadotropin", pp. 1028-1032, 1979, J. Biol. Chem., vol. 4, Feb.
Oeltmann, "Synthesis and In Vitro Activity of a Hormone-Diphtheria Toxin Fragment of a Hybrid", pp. 430-435, 1985, Biochem. Biophys. Res. Commun., vol. 133, Dec.
Pastan et al., "Immunotoxins", pp. 641-648, 1986, Cell, vol. 47, Dec.
Pineda M. H. et al., "Atrophy of Rabbit Testes Associated with Production of Antiserum to Bovine Luteinizing Hormone", pp. 665-668, 1967, Proc. Soc. Exp. Bio. Med., vol. 125, No. 3, Jul.
Quadri, S. K. et al., "Inhibition of Spermatogenesis and Ovulation in Rabbits With Antiovine LH Rabbit Serum", pp. 809-814, 1966, Proc. Soc. Exp. Bio. Med., vol. 123.
Schwartz et al., "A New Cytotoxin Specific for the Target Cells of Corticotropin-Releasing Factor", pp. 1454-1460, 1987, Endocrinology, vol. 121.
Singh et al., "Controlled Release of LHRH-DT From Bioerodible Hydrogel Microspheres", pp. R5-R8, 1991, International Journal of Pharmacology.
Tallgat M. et al., "Impairment of Spermatogenesis And Libido Through Antibodies to Luteinizing Hormone", pp. 113-118, 1971, Fertility and Sterility, vol. 22, No. 2, Feb.
Vitetta et al., "Redesigning Nature's Poisons to Create Anti-Tumor Reagents", pp. 1098-1104, 1987, Science, vol. 238, Nov.
Youle et al., "Immunotoxins Show Rapid Entry of Diphtheria Toxin but not Ricin via the T3 Antigen", pp. 93-98, 1986, J. Immunol., vol. 136, Jan.

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

Method for sterilizing animals using hormone-toxin conjugate com does not yet have a rating. At this time, there are no reviews or comments for this patent.

If you have personal experience with Method for sterilizing animals using hormone-toxin conjugate com, we encourage you to share that experience with our LandOfFree.com community. Your opinion is very important and Method for sterilizing animals using hormone-toxin conjugate com will most certainly appreciate the feedback.

Rate now

     

Profile ID: LFUS-PAI-O-156632

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