Antigenic modification of polypeptides
AssigneeThe Ohio State University Research Foundation
InventorVernon C. Stevens
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AssigneeThe Ohio State University Research Foundation
InventorVernon C. Stevens
Estimating the term…
Endogenous and exogenous proteins, and fragments thereof, are chemically modified outside the body of an animal so that when injected into the animal they produce more antibodies against the unmodified protein than would injection of the unmodified protein or fragment alone. The chemical modification may be accomplished by attaching the proteins or fragments to carriers such as, for example, bacterial toxoids. The chemical modification can also be accomplished by polymerization of protein fragments. Proteins which can be modified include Follicle Stimulating Hormone and Human Chorionic Gonadotropin. The modified polypeptides may be administered to animals for the purpose of contraception, abortion or treatment of hormone-related disease states and disease disorders, treatment of hormone-associated carcinomas, and to boost the animals resistance to exogenous proteins, for example viral proteins.
A modified polypeptide for isoimmunologically controlling biological action in a mammal by antibody formation, the modified polypeptide comprising a peptide having an amino acid sequence substantially similar to the region of a mammalian lutenizing hormone, chorionic gonadotropin, follicle secreting hormone or thyroid stimulating hormone corresponding to the 38-57 region of the beta-subunit of human chorionic gonadotropin, said peptide having the two cysteine residues corresponding to the cysteine residues at positions 38 and 57 of the beta-subunit of human chorionic gonadotropin having their sulfur atoms linked in a disulfide bridge, said peptide having been chemically modified outside the body of said mammal, said peptide having the properties of:
A modified polypeptide for isoimmunologically controlling biological action in a mammal by antibody formation, the modified polypeptide comprising a peptide having an amino acid sequence in its unmodified form of:
Dependencies are inferred from the claim text.