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Abstract
The binding property of bovine IgG2 to staphylococcal Protein A was investigated by the methods of gel filtration chromatography and affinity chromatography. High performance gel filtration chromatography was carried out using TSK gel G3000SW and G2000SW columns, and immobilized Protein A column was used for affinity chromatography. Although bovine IgG2 did not form any precipitin lines with Protein A by double diffusion method on agar gel, IgG2 could bind to immobilized Protein A column. Moreover, by gel filtration chromatography, peaks of the complex between bovine IgG2 and Protein A were observed in addition to the IgG2 monomer peak. Thus, it is concluded that bovine IgG2 interacts with staphylococcal Protein A and forms “soluble complexes”. Carbethoxylated IgG2 lost its affinity to Protein A indicating that histidyl residues in IgG2 is essential for the binding to Protein A.
References
- Mechanism of poly(ethylene glycol) interaction with proteins.Biochemistry. 1985; 24: 6756
Arata, Y. 1986. Structure and function of immunoglobulins. Tanpakusitsu Kakusan Kouso 31:782. (In Japanese.)
- Cow milk proteins: twenty five years of progress.J. Dairy Sci. 1981; 64: 1038
- Physicochemical and immuno-chemical studies on bovine IgA and glycoprotein-a.Biochem. Biophys. Acta. 1971; 251: 435
- Preparation of bovine immunoglobulins and free secretory component and their specific antisera.J. Dairy Sci. 1972; 55: 151
- Critical aspects of immune complex assays employing polyethylene glycol.J. Immunol. Methods. 1983; 60: 289
- Protein A from S. aureus. I. Pseudo-immune reaction with human gamma-globulin.J. Immunol. 1966; 97: 822
- Protein A reactivity of various mammalian immunoglobulins.Scand. J. Immunol. 1978; 8: 21
- The modification of human immunoglobulin binding to staphylococcal Protein A using diethyl pyrocarbonate.J. Immunol. 1982; 129: 190
- Electron microscopic and hydrodynamic studies of protein A-immunoglobulin G soluble complexes.J. Immunol. 1984; 132: 1386
- A model for the formation and interconversion of protein A-immunoglobulin G soluble complexes.J. Immunol. 1984; 132: 1397
- Phylogenetic insight into evolution of mammalian Fc fragment of gamma G globulin using staphylococcal Protein A.J. Immunol. 1970; 104: 140
- Variation in staphylococcal Protein A reactivity with gamma G- globulins of different species.Acta Pathol. Microbiol. Scand. 1970; B78: 673
- Modification of histidyl residues in proteins by diethylpyrocarbonate.in: Methods in enzymology. Vol. 47. Academic Press Inc., New York, NY1977: 431
- Characterization of the soluble complex formed by reacting rabbit IgG with protein A of S. aureus.Immunochemistry. 1978; 15: 639
Shimazaki, K., and K. Sukegawa. 1981. Comparison of binding amounts of bovine immunoglobulin G1 and G2 to Staphylococ cusaureus. Nippon Chikusan Gakkaiho 52:425. (In Japanese.)
- Binding properties of bovine milk immunoglobulins with staphylococci.in: Proc. Vth World Conf. Anim. Prod, Tokyo, Jpn.1983: 653
- Protein A isolated from Staphylococcus aureus after digestion with lysostaphin.Eur. J. Biochem. 1972; 29: 572
- Incomplete inhibition of the immunoglobulin G-binding behavior of nitrated Protein A.Infect. Immun. 1978; 21: 659
- Protein A: nature's universal anti-antibody.Trend Biochem. Sci. 1982; 7: 74
Article info
Publication history
Accepted:
September 15,
1988
Received:
November 19,
1987
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Copyright
© 1989 American Dairy Science Association. Published by Elsevier Inc.
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