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Anti-idiotypic Antibodies against Bovine Growth Hormone
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 Title & Authors
Anti-idiotypic Antibodies against Bovine Growth Hormone
Verma, N.K.; Sodhi, R.; Rajput, Y.S.;
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Anti-antibodies against three mouse monoclonal antibodies viz. IIB5D6, VIA6E8 and VIC1F9 (specific to bovine growth hormone) in rabbits have been generated and characterized. Ammonium sulfate fractionated and affinity-purified monoclonal antibodies were used for producing anti-antibodies. The generated anti-antibodies were against common as well as uncommon antigenic determinants present in mouse monoclonal antibodies. The raised anti-antibodies replaced [ ]bGH bound to goat liver microsomes indicating production of anti-idiotypic antibodies against bovine growth hormone. These antibodies can have profound implications in vivo in lactating bovines for enhancing milk yield.
Anti-idiotypic Antibodies;Bovine Growth Hormone;Bovine Somatotropin;Receptor Assay;Antibody Purification;
 Cited by
Amit, T., R. J. Barkey, M. Garish and M. B. H. Youdin. 1986. Antiidiotypic antibodies raised against anti-prolactin (PRL) antibodies recognize the PRL receptor. Endocrinology. 118:835-843. crossref(new window)

Baker, J. R., Y. G. Lukes and K. D. Burman. 1984. Production, isolation and characterisation of rabbit anti-idiotypic antibodies directed against human anti-thyrotropin receptor antibodies. J. Clin. Invest. 74:489-495.

Bradford, M. M. 1976. A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal. Biochem. 72:248-254. crossref(new window)

Cadman, H. F. and M. Wallis. 1981. An investigation of the sites that bind human somatotropin in the liver of pregnant rabbit. Biochem. J. 198:605-610..

Chen, P. P., R. A. Houghton, S. Fong, G. H. Rhodes, T. A. Gilbertson, J. H. Vaughan, R. A. Lerner, and D. A.Carson. 1984. Anti-hypervariable region antibody induced by a defined peptide: An approach foe studying the structural correlates of idiotopes. Proc Natl. Acad. Sci. USA 81:1784-1788. crossref(new window)

Elbashir, M. I., T. Brodin, Akerström and J. Donner. 1990. Monoclonal antibodies to the pituitary growth-hormone receptor by the anti-idiotypic approach-production and initial characterization. Biochem. J. 266:467-474.

Emtner, M., J. Brandt, U. Johanson, B. Jruper, L. Fryklund and P. Roos. 1989. A monoclonal antibody to lactogenic receptors from female rat liver. J. Endcrinol. 120:401-407. crossref(new window)

Engvall, E., and P. Perlman. 1971. Enzyme linked immunosorbent assay (ELISA)-quantitative assay of immunoglobulin G. Immunochemistry, 8:871-874. crossref(new window)

Erp, R. V., M. Adorf, A. P. G. Van Sommeren and T. C. J. Gribnau. 1991a. Monitoring of the production of monoclonal antibodies by hybridoma. Part I: Long-term cultivation in hollow fibre bioreactors using serum-free medium. J. Biotech. 20:249-262. crossref(new window)

Erp, R. V., M. Adorf, A. P. G. Van Sommeren, O. T. Schonherr and T. C. J. Gribnau. 1991b. Monitoring of the production of monoclonal antibodies by hybridoma. Part II: Characterization and purification of acid proteases present in cell culture supernatant. Biotechnology 20:235-248. crossref(new window)

Ferrara, P., M. M. Zakim, C. Pena and A. C. Paladini. 1979. Immunologically active zones in bovine growth hormone. Eur. J Immunol., 9:1020-1023. crossref(new window)

Fraker, P. J. and J. C. Speck. 1978. Protein and cell membrane iodinations with a sparingly soluble chloroamide 1, 3, 4, 6-tetrachloro-3$\alpha$, 6$\alpha$ diphenyl glycouril. Biochem. Biophys. Res. Comm. 80:849-857. crossref(new window)

Gardner, M. J., C. A. Morrison, L. Q. Stevenson and D. J. Flint. 1990. Production of anti-idiotypic antisera to rat GH antibodies capable of binding to GH receptors and increasing body weight gain in hypophysectomised rats. J. Endocrinol. 125:53-59. crossref(new window)

Harlow, E. and D. Lane. 1988. Antibodies: A laboratory Manual, Cold Spring Harbor Laboratory, New York.

Haro, L. S., R. J. Collier and F. J. Talamantes. 1984. Homologous somatotropin radioreceptor assay utilizing recombinant bovine growth hormone. Mol. Cell. Endocrinol. 38:109-116. crossref(new window)

Jerne, N. K. 1974. Towards a network theory of the immune system.Annales d' Immunologie, 125C:373-389

Kumar, P. and Y. S. Rajput. 1999. Monoclonal antibodies against bovine growth hormone. Ind. J. Exptl. Biol. 37:650-654.

Laemmli, U. K. 1970. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 227:680-685. crossref(new window)

Lee, S-M. 1987. Affinity purification of monoclonal antibody from tissue culture supernatant usinf protein A-Sepharose CL-4B. In: Commercial production of monoclonal antibodies. (Ed. S. S. Seaver). Marcell Dekker, Inc., New York. pp.199-217

Mor, G., Y. Amir-Zaltsman, G. Barnard and F. Kohen. 1992. Characteristics of an antiidiotypic antibody minimizing the actions of estradiol and its interaction with estrogen receptors. Endocrinology 130:3633-3640. crossref(new window)

Nilsson, L. A. 1984. Handbook of immunoprecipittion-in-gel techniques. N. H. Axelson (Ed.). Blackwell scientific Publications, Oxford. pp.57-68.

Sairam, M. R., G. N. Bhargavi and B. R. Downer. 1992.Biological mimicry of gonadotropin action by antiidiotypic antibodies to lutinizing hormone: Characterization and biological properties. Endocrinology 131:1212-1222. crossref(new window)

Schalla, C. L., S. Roberge, B. N. Wilkie, B. W. McBride and J. S. Walton. 1994. Production of anti-idiotypic antibodies resembling bovine somatotopin by active immunization of lactating cows. J. Endocrinol. 141:203-208. crossref(new window)

Sodhi, R. and Y. S. Rajput. 2001. Mechanism of growth hormone action: Recent developments. Asian Aust. J. Anim. Sci. 14:1785-1793.

Udupa, T. N. S. and A. R. Sheth. 1987. Binding of anti-idiotypic antibodies against anti-FSH to FSH receptors. Ind. J. Exptl Biol. 25:290-292.

Wallis, M. 1988. Mechanism of action of growth hormone. In: Hormones and their Actions, PartII B. A. Cooke, R. J. B. King and H. J. Vander Molen (Ed.). Elsevier Science Publishers. pp. 265-290.

Wells, J. A. and A. M. deVos. 1996. Hematopoietic receptor complexes. Ann. Rev. Biochem. 65:609-634. crossref(new window)