Abstract
The type of gene duplication which produced the group of isozyme genes contributed greatly to the evolution of increasingly complex organisms. These functionally diverged duplicated genes, however, still specify the same enzyme in that their products act upon the same substrate with the help of the same coenzyme. A, B and C-subunits of LDH of any vertebrate must still maintain either the identical active site sequence of 12 amino acids (— Val-Ile-Ser-Gly-Gly-Cys-Asn-Leu-Asp-Thr-Ala-Arg —), or a sequence very similar to the above, for this is the sequence which binds with NAD and recognizes pyruvate or lactate as the substrate (Kaplan, 1965). Differences in the kinetic property of A, B and C-subunits must reflect amino acid substitutions which affect sites other than the active site of the polypeptide chain.
Access this chapter
Tax calculation will be finalised at checkout
Purchases are for personal use only
Preview
Unable to display preview. Download preview PDF.
References
Baglioni, C.: Homologies in the position of cysteine residues of K and L type chains of human immunoglobins. Biochem. Biophys. Res. Commun. 26, 82–89 (1967).
Black, J.A., Dixon, G.H.: Amino-acid sequence of alpha chain of human haptoglobins. Nature 218, 736–741 (1968).
Borisy, G.G., Taylor, E.W.: The mechanism of action of colchicine: binding of colchicine-3H to cellular protein. J. Cell Biol. 34, 523–533 (1967).
Burnet, F.M.: The clonal selection theory of acquired immunity. London: Cambridge Univ. Press 1958.
Doolittle, R.F., Singer, S.J., Metzger, H.: Evolution of immunoglobulin polypeptide chains: Carboxyterminal of an IgM heavy chain. Science 154, 1561–1562 (1966).
Edmundson, A.B.: Amino-acid sequence of sperm whale myoglobin. Nature 205, 883–887 (1965).
Eigsti, O.J., Dustin, P., Jr.: Colchicine in agriculture, medicine, biology and chemistry. Ames (Iowa): Iowa State College Press 1955.
Glick, B., Chang, T.S., Jaap, R.G.: The bursa of Fabricius and antibody production. Poultry Sci. 35, 224–234 (1956).
Gray, W., Dreyer, W., Hood, L.: Mechanism of antibody synthesis: Size difference between mouse kappa chains. Science 155, 465–467 (1967).
Hildemann, W.H., Thoenes, G.H.: Immunological response of Pacific hagfish. I. Skin transplantation immunity. Transplantation 7, 506–529 (1969).
Hilschmann, N., Craig, L.C.: Amino acid sequence studies with Bence-Jones proteins. Proc. Natl. Acad. Sci. US 53, 1403–1409 (1965).
Hilse, K., Sorger, U., Braunitzer, G.: Zur Phylogenie des Hämoglobinmoleküls über den Polymorphismus und die N-terminalen Aminosäuren des Karpfenhämoglobins. Z. physiol. Chem., Hoppe Seyler’s 344, 166–168 (1966).
Ingram, V.M.: The hemoglobin in genetics and evolution. New York: Columbia University Press 1963.
Kaplan, N.O.: Evolution of dehydrogenases. In: Evolving genes and proteins (Bryson, W., Vogel, H.J., Eds.). New York: Academic Press 1965.
Kauffman, D.L.: The disulphide bridges of trypsin. J. Mol. Biol. 12, 929–932 (1965).
Keil, B., Prusik, Z., Šorm, F.: Disulphide bridges and a suggested structure of chymotrypsinogen. Biochim. et Biophys. Acta 78, 559–561 (1963).
Kendrew, J.C., Dickerson, R.E., Strandberg, B.E., Hart, R.G., Davies, D.R., Phillips, D.C., Shore, U.C.: Structure of myoglobin: A three-dimensional fourier synthesis at 2Å resolution obtained by X-ray analysis. Nature 185, 422–427 (1960).
Lennox, E., Cohn, M.: Immunoglobin genetics. Ann. Rev. Biochem. 36, 365–406 (1967).
Marchalonis, J., Edelman, G.M.: (1) Polypeptide chains of immunoglobulins from the smooth dogfish (Mustelus canis). Science 154, 1567–1568 (1966).
— (2) Phylogenetic origins of antibody structure. II. Immunoglobulins in the primary immune response of the bullfrog, Rana catesbiana. J. Exptl. Med. 124, 901–913 (1966).
Margoliash, E.: Primary structure and evolution of cytochrome C. Proc. Natl. Acad. Sci. US 50, 672–679 (1963).
Miller, J.F.A.P.: Immunological function of the thymus. Lancet 1961 II, 748–749.
Milstein, C.: The disulphide bridges of immunoglobulin ϰ-chains. Biochem. J. 101, 338–351 (1966).
Neurath, H., Walsh, K.A., Winter, W.P.: Evolution of structure and function of proteases. Science 158, 1638–1644 (1967).
Ohno, S., Morrison, M.: Multiple gene loci for the monomeric hemoglobin of the hagfish (Eptatretus stoutii). Science 154, 1034–1035 (1966)
Okazaki, K., Holtzer, H.: Aspects of myogenesis in vitro. J. Cell Biol. 27, 75A (1965).
Papermaster, B.W., Condie, R.M., Finstad, J., Good, R.A.: Immune response in the California hagfish. Nature 196, 355–356 (1962).
Perutz, M.F., Rossmann, M.B., Cullis, A.F., Muirhead, H., Will, G., North, A.C.T.: Structure of hemoglobin: A three dimensional fourier synthesis at 5.5 Å resolution, obtained by X-ray analysis. Nature 185, 416–422 (1960).
Porter, R.R.: A discussion of the chemistry and biology of immunoglobulins. Proc. Roy. Soc. (London), B 166, 113–243 (1966).
Renaud, F.L., Rowe, A.J., Gibbons, I.R.: Some properties of the protein forming the outer fibers of cilia. J. Cell Biol. 36, 79–90 (1968).
Rudloff, V., Zelenik, M., Braunitzer, G.: Zur Phylogenie des Hämoglobinmoleküls, Untersuchungen am Hämoglobin des Flußneunauges (Lampetra fluviatilis). Z. physiol. Chem., Hoppe Seyler’s 344, 284–288 (1966).
Shelansky, M.L., Taylor, E.W.: Properties of the protein subunit of central-pair and outer-doublet microtubulues of sea urchin flagella. J. Cell Biol. 38, 304–315 (1968).
Szent-Györgyi, A.: Chemistry of muscular contraction. New York: Academic Press 1957.
Tilney, L.G., Hiramoto, Y., Marsland, G.: Studies on the microtubules in heliozoa. III. A pressure analysis of the role of these structures in the formation and maintenance of the axopidia of Actinosphaerium nucleofilum (Barrett). J. Cell Biol. 29, 77–95 (1966).
Weisenberg, R.C., Borisy, G.G., Taylor, E.W.: The colchicine-binding protein of mammalian brain and its relation to microtubules. Biochem. J. 7, 4466–4479 (1968).
Wikler, M., Köhler, H., Shinoda, T., Putnam, F.W.: Macroglobulin structute: Homology of Mu and gamma heavy chains of human immunoglobulin. Science 163, 75–78 (1969).
Author information
Authors and Affiliations
Rights and permissions
Copyright information
© 1970 Springer Science+Business Media New York
About this chapter
Cite this chapter
Ohno, S. (1970). The Creation of a New Gene from a Redundant Duplicate of an Old Gene. In: Evolution by Gene Duplication. Springer, Berlin, Heidelberg. https://doi.org/10.1007/978-3-642-86659-3_14
Download citation
DOI: https://doi.org/10.1007/978-3-642-86659-3_14
Publisher Name: Springer, Berlin, Heidelberg
Print ISBN: 978-3-642-86661-6
Online ISBN: 978-3-642-86659-3
eBook Packages: Springer Book Archive