Abstract
The optical rotations of solutions of the antigen—antibody complexes formed by excess of antigen were measured over a range of wave-lengths. The antigens used were bovine serum albumin (BSA) and diphtheria toxin. A method of estimating the optical rotations of the precipitable antibody against BSA in a solution of rabbit γG-globulin was used. The antitoxin used was isolated peptic antitoxin.
The optical rotations found were compared with those anticipated if the optical rotations had not been altered on combination. The optical rotation of the BSA—antibody complex at the D-line did not differ appreciably from that anticipated, but differences were found at shorter wave-lengths.
Mixtures of toxin and peptic antitoxin, in which the molecular ratios of toxin to antitoxin ranged from 2.29 to 0.37, gave rotatory dispersion curves, in the far ultraviolet range, which differed from those of the sums of the separate specific rotations of the constituent toxin, free and combined, and antitoxin. The differences in position and amplitude of peaks and troughs depended on the ratio of toxin to antitoxin. But in every mixture the maximum specific rotation at 205–210 mμ was less than the anticipated maximum rotation. Over the range 230–250 mμ the observed specific rotations of the mixture in which the ratio of toxin to antitoxin was highest were less negative than the anticipated specific rotations; in the mixture in which the ratio of toxin to antitoxin was lowest the observed rotations over the range 225–400 mμ were more negative than those anticipated.
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Selected References
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- BRESLOW E., BEYCHOK S., HARDMAN K. D., GURD F. R. RELATIVE CONFORMATIONS OF SPERM WHALE METMYOGLOBIN AND APOMYOGLOBIN IN SOLUTION. J Biol Chem. 1965 Jan;240:304–309. [PubMed] [Google Scholar]
- CRUMPTON M. J., POLSON A. A COMPARISON OF THE CONFORMATION OF SPERM WHALE METMYOGLOBIN WITH THAT OF APOMYOGLOBIN. J Mol Biol. 1965 Apr;11:722–729. doi: 10.1016/s0022-2836(65)80030-4. [DOI] [PubMed] [Google Scholar]
- Davidson B., Tooney N., Fasman G. D. The optical rotatory dispersion of the beta structure of poly-L-lysine and poly-L-serine. Biochem Biophys Res Commun. 1966 Apr 19;23(2):156–162. doi: 10.1016/0006-291x(66)90521-3. [DOI] [PubMed] [Google Scholar]
- Fujio H., Karush F. Antibody affinity. II. Effect of immunization interval on antihapten antibody in the rabbit. Biochemistry. 1966 Jun;5(6):1856–1863. doi: 10.1021/bi00870a011. [DOI] [PubMed] [Google Scholar]
- GELL P. G., KELUS A. S. ANTI-ANTIBODY OR CLONE-PRODUCT? Nature. 1964 Feb 15;201:687–689. doi: 10.1038/201687a0. [DOI] [PubMed] [Google Scholar]
- GOULD H. J., GILL T. J., 3rd, DOTY P. THE CONFORMATION AND HYDROGEN ION EQUILIBRIUM OF NORMAL RABBIT GAMMA-GLOBULIN. J Biol Chem. 1964 Sep;239:2842–2851. [PubMed] [Google Scholar]
- GRABAR P., ROBERT B. Dosage des groupements thiol protéiques dans des réactions immunochimiques. Ann Inst Pasteur (Paris) 1957 Jan;92(1):56–61. [PubMed] [Google Scholar]
- Henney C. S., Stanworth D. R., Gell P. G. Demonstration of the exposure of new antigenic determinants following antigen-antibody combination. Nature. 1965 Mar 13;205(976):1079–1081. doi: 10.1038/2051079a0. [DOI] [PubMed] [Google Scholar]
- IMAHORI K. Rotatory behavior of protein denaturation. Biochim Biophys Acta. 1960 Jan 15;37:336–341. doi: 10.1016/0006-3002(60)90242-0. [DOI] [PubMed] [Google Scholar]
- JIRGENSONS B. THE COTTON EFFECTS IN THE OPTICAL ROTATORY DISPERSION OF PROTEINS AS NEW CRITERIA OF CONFORMATION. J Biol Chem. 1965 Mar;240:1064–1071. [PubMed] [Google Scholar]
- Jirgensons B. Optical rotatory dispersion of nonhelical proteins. J Biol Chem. 1966 Jan 10;241(1):147–152. [PubMed] [Google Scholar]
- Kekwick R. A. The serum proteins in multiple myelomatosis. Biochem J. 1940 Sep;34(8-9):1248–1257. doi: 10.1042/bj0341248. [DOI] [PMC free article] [PubMed] [Google Scholar]
- MARRACK J. R., HOCH H., JOHNS R. G. S. The valency of antibodies. Br J Exp Pathol. 1951 Jun;32(3):212–230. [PMC free article] [PubMed] [Google Scholar]
- NOELKEN M. E., NELSON C. A., BUCKLEY C. E., 3rd, TANFORD C. GROSS CONFORMATION OF RABBIT 7 S GAMMA-IMMUNOGLOBULIN AND ITS PAPAIN-CLEAVED FRAGMENTS. J Biol Chem. 1965 Jan;240:218–224. [PubMed] [Google Scholar]
- POULIK M. D. Interaction of transferrin, haptoglobin and other serum proteins with neuraminidase of diphtheria toxin. Clin Chim Acta. 1961 Jul;6:493–502. doi: 10.1016/0009-8981(61)90138-3. [DOI] [PubMed] [Google Scholar]
- RAYNAUD M., BIZZINI B., RELYVELD E. H. COMPOSITION EN AMINO-ACIDES DE LA TOXINE DIPHT'ERIQUE PURIFI'EE. Bull Soc Chim Biol (Paris) 1965;47:261–266. [PubMed] [Google Scholar]
- Riddiford L. M. Solvent perturbation and ultraviolet optical rotatory dispersion studies of paramyosin. J Biol Chem. 1966 Jun 25;241(12):2792–2802. [PubMed] [Google Scholar]
- Ross D. L., Jirgensons B. The far ultraviolet optical rotatory dispersion, circular dichroism, and absorption spectra of a myeloma immunoglobulin, immunoglobulin G. J Biol Chem. 1968 May 25;243(10):2829–2836. [PubMed] [Google Scholar]
- Ruttenberg M. A., King T. P., Craig L. C. The use of the tyrocidines for the study of conformation and aggregation behavior. J Am Chem Soc. 1965 Sep 20;87(18):4196–4198. doi: 10.1021/ja01096a040. [DOI] [PubMed] [Google Scholar]
- STRAUB F. B. FORMATION OF THE SECONDARY AND TERTIARY STRUCTURE OF ENZYMES. Adv Enzymol Relat Areas Mol Biol. 1964;26:89–114. doi: 10.1002/9780470122716.ch3. [DOI] [PubMed] [Google Scholar]
- Schultze H. E., Haupt H., Heide K., Heimburger N., Schwick H. G. Comparative investigations of purified diphtheria and tetanus T-components and their fragments. Immunochemistry. 1965 Sep;2(3):273–284. doi: 10.1016/0019-2791(65)90007-8. [DOI] [PubMed] [Google Scholar]
- Steiner L. A., Lowey S. Optical rotatory dispersion studies of rabbit gamma-G-immunoglobulin and its papain fragments. J Biol Chem. 1966 Jan 10;241(1):231–240. [PubMed] [Google Scholar]
- Telser A., Robinson H. C., Dorfman A. The biosynthesis of chondroitin-sulfate protein complex. Proc Natl Acad Sci U S A. 1965 Sep;54(3):912–919. doi: 10.1073/pnas.54.3.912. [DOI] [PMC free article] [PubMed] [Google Scholar]
- URNES P. J., IMAHORI K., DOTY P. The optical rotatory dispersion of right-handed alpha-helices in sperm whale myoglobin. Proc Natl Acad Sci U S A. 1961 Oct 15;47:1635–1641. doi: 10.1073/pnas.47.10.1635. [DOI] [PMC free article] [PubMed] [Google Scholar]
- URNES P., DOTY P. Optical rotation and the conformation of polypeptides and proteins. Adv Protein Chem. 1961;16:401–544. doi: 10.1016/s0065-3233(08)60033-9. [DOI] [PubMed] [Google Scholar]
- Yang J. T., McCabe W. J. On the magnitude of the cotton effects of poly-L-glutamic acid. Biopolymers. 1965;3(2):209–212. doi: 10.1002/bip.360030208. [DOI] [PubMed] [Google Scholar]
