Skip to main content

Physiology and Biochemistry of Enzyme Variation: The Interface of Ecology and Population Genetics

  • Conference paper
Ecological Genetics: The Interface

Part of the book series: Proceedings in Life Sciences ((LIFE SCIENCES))

Abstract

“That is to say, the genes in question, insignificant as are their visible effects, have an important influence on the physiology of the organism, modifying profoundly the individual as a unit upon which selection operates.” E.B. Ford, 1965.

This is a preview of subscription content, log in via an institution to check access.

Access this chapter

Chapter
USD 29.95
Price excludes VAT (USA)
  • Available as PDF
  • Read on any device
  • Instant download
  • Own it forever
eBook
USD 84.99
Price excludes VAT (USA)
  • Available as PDF
  • Read on any device
  • Instant download
  • Own it forever
Softcover Book
USD 109.99
Price excludes VAT (USA)
  • Compact, lightweight edition
  • Dispatched in 3 to 5 business days
  • Free shipping worldwide - see info

Tax calculation will be finalised at checkout

Purchases are for personal use only

Institutional subscriptions

Preview

Unable to display preview. Download preview PDF.

Unable to display preview. Download preview PDF.

References

  • Adibi, S.A., Mercer, D.W.: Protein digestion in human intestine as reflected in luminal, mucosal, and plasma amino acid concentrations after meals. J. Clin. Invest. 52:1594–1596. (1973).

    Article  Google Scholar 

  • Ayala, F.J. (ed.): Molecular Evolution. Sunderland, Mass.: Sinnauer Assoc., Inc., 1976, p. 277.

    Google Scholar 

  • Barrett, A.J., Dingle, J.T. (eds.): Tissue Proteinases. Amsterdam: North-Holland Publ. Co., 1971, p. 353.

    Google Scholar 

  • Bayne, B.L., Widdows, J., Thompson, R.J.: Physiology II. In Marine Mussels: Their Ecology and Physiology, (ed. B. Bayne). Cambridge: Cambridge University Press, 1976, pp. 207–260.

    Google Scholar 

  • Bishop, S.H.: Nitrogen metabolism and excretion: Regulation of intracellular amino acid concentrations. In Estuarine Processes, Vol. I. (ed. M. Wiley). New York: Academic Press, 1976.

    Google Scholar 

  • Brieteux-Gregoire, S., Duchateau-Bosson, G., Jeuniaux, C., Florkin, M.: Constituants osmotiquement actifs des muscles adducteurs de Mytilus edulis adaptee a l’eau ou a l’eau saumatre. Arch. Int. Physiol. Biochem. 72:116–123. (1964).

    Article  Google Scholar 

  • Bryant, E.H.: On the adaptive significance of enzyme polymorphism in relation to environmental variability. Amer. Natur. 108:1–19. (1974).

    Article  Google Scholar 

  • Day, T.H., Hillier, P.C., Clarke, B.: Properties of genetically polymorphic isozymes of alcohol dehydrogenase in Drosophila melanogaster. Biochem. Genet. 11:141–153. (1974a).

    Article  PubMed  CAS  Google Scholar 

  • Day, T.H., Hillier, P.C., Clarke, B.: The relative quantities and catalytic activities of enzymes produced by alleles at the alcohol dehydrogenase locus inDrosophila melanogaster. Biochem. Genet. 11:155–165. (1974b).

    Article  PubMed  CAS  Google Scholar 

  • Day, T.H., Needham, L.: Properties of alcohol dehydrogenase isozymes in a strain of Drosophila melanogaster homozygous for the Adh- slow allele. Biochem. Genet. 11:167–175. (1974).

    Article  PubMed  CAS  Google Scholar 

  • Ford, E.B.: Genetic Polymorphism. All Soul’s Studies. London: Faber and Faber, 1965, p. 101.

    Google Scholar 

  • Gibson, J.: Enzyme flexibility in Drosophila melanogaster. Nature 227:959–960. (1970).

    Article  PubMed  CAS  Google Scholar 

  • Hedrick, P.W., Ginevan, M.R., Swing, E.P.: Genetic polymorphism in heterogeneous environments. Ann Rev. Ecol. Syst. 2. (1976).

    Google Scholar 

  • Kim, M.S., Brohpy, E.J.: Rat intestinal brush border membrane peptidases. I. Solubilization, purification, and physicochemical properties of two different forms of the enzyme. J. Biol. Chem. 251:3199–3205. (1976).

    PubMed  CAS  Google Scholar 

  • Kim, Y.S. McCarthy, D.M., Lane, W., Fong, W.: Alterations in the levels of peptide hydrolases and other enzymes in brush-border and soluble fractions of rat small intestinal mucosa during starvation and refeeding. Biochem. Biophys. Acta 321:262–273. (1973).

    PubMed  CAS  Google Scholar 

  • Kim, Y.S., Kim, Y.W., Sleisenger, M.H.: Studies on the properties of peptide hydrolases in the brush-border and soluble fractions of small intestinal mucosa of rat and man. Biochem. Biophys. Acta 370:283–296. (1974a).

    PubMed  CAS  Google Scholar 

  • Kim, Y.S., Nicholson, J.A., Curtis, K.J.: Intestinal peptide hydrolases: Peptide and amino acid absorption. Med. Slin. N. Amer. 58:1397–1412. (1974b).

    CAS  Google Scholar 

  • Koehn, R.K.: Esterase heterogeneity: Dynamics of a polymorphism. Science 163:943–944. (1969).

    Article  PubMed  CAS  Google Scholar 

  • Koehn, R.K.: Biochemical aspects of genetic variation at the LAP locus in Mytilus edulis. In The Genetics of Marine Organisms, (eds. B. Battaghlia and J.A. Beardmore). New York: Plenum Press, 1978.

    Google Scholar 

  • Koehn, R.K., Mitton, J.B.: Population genetics of marine pelecypods. I. Ecological heterogeneity and evolutionary strategy at an enzyme locus. Amer. Natur. 106:47–56. (1972).

    Article  Google Scholar 

  • Koehn, R.K., Milkman, R., Mitton, J.B.: Population genetics of marine pelecypods. IV. Selection, migration and genetic differentiation in the Blue Mussel, Mytilus edulis. Evolution 30:2–32. (1976).

    Article  Google Scholar 

  • Levene, H.: Genetic equilibrium when more than one niche is available. Amer. Natur. 82:331–333. (1953).

    Google Scholar 

  • Levins, R.: Evolution in Changing Environments. Princeton, New Jersey: Princeton University Press, 1968, p. 120.

    Google Scholar 

  • Levinton, J.S., Koehn, R.K.: Population genetics of mussels. In Marine Mussels: Their Ecology and Physiology. (ed. B.L. Bayne). Cambridge: Cambridge University Press, 1976, pp. 357–384.

    Google Scholar 

  • Lewontin, R.C.: The Genetic Basis of Evolutionary Change. New York: Columbia University Press, 1974, p. 346.

    Google Scholar 

  • Maroux, S., Louvard, D., Baratti, J.: The aminopeptidase from hog intestinal brush border. Biochim. Biophys. Acta 321:282–295. (1973).

    PubMed  CAS  Google Scholar 

  • Merritt, R.B.: Geographic distribution and enzymatic properties of lactate dehydrogenase allozymes in the Fathead Minnow, Pimaphales promelas. Amer. Natur. 196:173–184. (1972).

    Google Scholar 

  • Milkman, R., Koehn, R.K.: Temporal variation in the relationship between size, numbers and an allele-frequency in a population of Mytilus edulis. Evolution 31:103–115. (1977).

    Article  Google Scholar 

  • Miller, S., Pearcy, R.W., Berger, E.: Polymorphism at the a-glycero-phosphate dehydrogenase locus in Drosophila melanogaster. I. Properties of adult allozymes. Biochem. Genet. 13:175–188. (1975).

    Article  PubMed  CAS  Google Scholar 

  • Mitton, J.B., Koehn, R.K.: Population genetics of marine pelecypods. III. Epistasis between functionally related isoenzymes of Mytilus edulis. Genetics 73:487–496. (1973).

    PubMed  CAS  Google Scholar 

  • Nei, M.: Molecular Population Genetics and Evolution. Amsterdam: North-Holland Publ. Co., 1975, p. 288.

    Google Scholar 

  • Pierce, S.K.: Volume regulation and valve movements by marine mussels. Comp. Biochem. Physiol. 39A:103–117. (1971).

    Article  Google Scholar 

  • Piggott, C.O., Fottrell, P.F.: Purification and characterization from guinea-pig intestinal mucosa of two peptide hydrolases which preferentially hydrolyse dipeptides. Biochim. Biophys. Acta 391:403–309. (1975).

    PubMed  CAS  Google Scholar 

  • Smyth, D.H.: Peptide transport by mammalian gut. In Peptide Transport in Bacteria and Mammalian Gut. Ciba Foundation Symposium. Amsterdam: Elsevier, Excerpta Medica, North-Holland, 1972, pp. 59–70.

    Google Scholar 

  • Somero, G.N., Low, P.S.: Eurytolerant proteins: Mechanisms for extending the environmental tolerance range of enzyme-ligand interactions. Amer. Natur. 111:527–538. (1977).

    Article  CAS  Google Scholar 

  • Thompson, R.J., Ratcliff, N.A., Bayne, B.L.: Effects of starvation on structure and function in the digestive gland of the mussel (Mytilus edulis L.). J. Mar. Biol. Assn. U.K. 54:699–712. (1974).

    Article  CAS  Google Scholar 

  • Thorig, G.E.W., Schoone, A.A., Scharloo, W.: Variation between electrophoretically identifiable alleles at the alcohol dehydrogenase locus in Dvosophila melanogaster. Biochem. Genet. 13:721–731. (1975).

    Article  PubMed  CAS  Google Scholar 

  • Vigue, C.L., Johnson, F.M.: Isozyme variability in species of the genus Drosophila. VI. Frequency-property-environment relationships of allelic alcohol dehydrogenases in D. melanogaster.Biochem. Genet. 9:213–228. (1973).

    Article  PubMed  CAS  Google Scholar 

  • Wojnarowska, F., Gray, G.M.: Intestinal surface peptide hydrolases: Identification and characterization of three enzymes from rat brush border. Biochim. Biophys. Acta 403:147–160. (1975).

    PubMed  CAS  Google Scholar 

  • Young, J.P.W., Koehn, R.K., Arnheim, N.: An aminopeptidase from the mussel, Mytilus edulis: Purification and properties. (MS in preparation, 1978).

    Google Scholar 

Download references

Authors

Editor information

Editors and Affiliations

Rights and permissions

Reprints and permissions

Copyright information

© 1978 Springer-Verlag New York Inc.

About this paper

Cite this paper

Koehn, R.K. (1978). Physiology and Biochemistry of Enzyme Variation: The Interface of Ecology and Population Genetics. In: Brussard, P.F. (eds) Ecological Genetics: The Interface. Proceedings in Life Sciences. Springer, New York, NY. https://doi.org/10.1007/978-1-4612-6330-2_3

Download citation

  • DOI: https://doi.org/10.1007/978-1-4612-6330-2_3

  • Publisher Name: Springer, New York, NY

  • Print ISBN: 978-1-4612-6332-6

  • Online ISBN: 978-1-4612-6330-2

  • eBook Packages: Springer Book Archive

Publish with us

Policies and ethics