Journal of Comparative Physiology B

, Volume 159, Issue 2, pp 237–242 | Cite as

Theamylase gene-enzyme system of fishes

II. Comparison of amylases from the mosquitofish, rat andDrosophila
  • Darrell G. Yardley


Amylases from the mosquitofish (Gambusia affinis holbrooki, Pisces: Poeciliidae) and rat were purified and compared withDrosophila amylases in terms of structure and function. At the structural level, amino acid compositions of the three amylases were compared. At the functional level, amylase activities were compared on various substrates and in the presence of inhibitors.

While the amylases from all three organisms had properties typical of alpha-amylases, both structural and functional differences were observed. Using resemblance coefficients of distance and similarity from numerical taxonomy, it was determined that the amylases from the rat andDrosophila were more similar to each other than either was to amylase from the mosquitofish, and that structural differences between the amylases did not reflect functional differences, i.e. there was no correlation between amylase structural and functional distances.

Key words

Amylase Mosquitofish Rat Drosophila Structure Function 


Unable to display preview. Download preview PDF.

Unable to display preview. Download preview PDF.


  1. Bradford MM (1976) A rapid and sensitive method for the quantification of microgram quantities of protein utilizing the principle of protein-dye binding. Analyt Biochem 72:248–254Google Scholar
  2. Chernin MI, Stevens SN, Kline EL, Yardley DG (1987) An amylase gene fromDrosophila pseudoobscura is expressed inEscherichia coli. Biochim Biophys Acta 910:63–71Google Scholar
  3. Doane WW (1969) Athylase variants inDrosophila melanogaster: linkage studies and characterization of enzyme extracts. J Exp Zool 171:321–342Google Scholar
  4. Doane WW, Abraham I, Kolar MM, Martenson RE, Diebler GE (1975) Purified drosophila α-amylase isozymes: genetical, biochemical and molecular characterization. In: Markert CL (ed) Isozymes: genetics and evolution, vol 4. AR Liss, New York, pp 585–607Google Scholar
  5. Herrera RJ (1979) Preferential gene expression of an amylase E.C. allele in interspecific hybrids ofXiphophorus (Pisces: Poeciliidae). Biochem Genet 17:223–227Google Scholar
  6. Hickey DA, Benkel BF, Boer PH, Genest Y, Abukashawa S, Ben-David G (1987) Enzyme-coding genes as molecular clocks: the molecular evolution of animal alpha-amylases. J Mol Evol 26:252–256Google Scholar
  7. Karn RC, Malacinsky GM (1978) The comparative biochemistry, physiology, and genetics of animal α-amylase. Adv Comp Physiol Biochem 7:1–103Google Scholar
  8. Kenyon WA (1925) Digestive enzymes in poikilothermal vertebrates — an investigation of enzymes in fishes with comprative studies on those of amphibians, reptiles and mammals. Bull Bur Fish 41:181–200Google Scholar
  9. Laemmli UK (1978) Cleavage of structural proteins during assembly of the head of bacteriophage T4. Nature 227:680–685Google Scholar
  10. Malacinski GM, Rutter WJ (1969) Multiple molecular forms of α-amylase from the rabbit. Biochemistry 8:4382–4390Google Scholar
  11. Nakajima R, Imanaka T, Aiba S (1986) Comparison of amino acid sequences of eleven different α-amylases. Appl Microbiol Biotechnol 23:355–360Google Scholar
  12. Sarbahi DS (1951) Studies on the digestive tracts and the digestive enzymes of the goldfish,Carassius auratus (Linn.) and largemouth bass,Micropterus salmoides (Lacepede). Biol Bull 66:244–257Google Scholar
  13. Silano V, Pocchairi F, Kasarda DD (1973) Physical characterization of α-amylase inhibitors from wheat. Biochim Biophys Acta 317:131–148Google Scholar
  14. Sinha GM (1978) Amylase, protease and lipase activities in the alimentary tract of fresh water major carp,Cirrhinus mrigala, during different life-history stages in relation to food and feeding habits. Zool Beitr 24:349–358Google Scholar
  15. Sluyterman LAE, Wijdenes J (1977) Chromatofocusing: isoelectric focusing on ion exchangers in the absence of an externally applied potential. In: Radola BJ, Graesslin D (eds) Proc Int Symp Electrofocusing and Isotachophoresis. De Gruyter, Berlin, pp 463–466Google Scholar
  16. Sneath PHA, Sokal RR (1973) Numerical taxonomy, WH Freeman, San Francisco, CAGoogle Scholar
  17. Thoma JA, Spradlin JE, Dygert S (1971) Plant and animal amylases. In: Boyer PD (ed) The enzymes, vol 5. Academic Press, New York, pp 115–189Google Scholar
  18. Vandermeers A, Christophe J (1968) α-amylase et lipase du pancreas de rat. Purification chromatographique, recherche du poids moleculaire et composition en acides amines. Biochim Biophys Acta 154:110–129Google Scholar
  19. Waite JH, Benedict CV (1984) Assay of dihydrophenylalanine (dopa) in invertebrate structural proteins. In: Wold F, Moldave K (eds) Methods in enzymology, vol 107. Academic Press, New York, pp 397–413Google Scholar
  20. Yardley DG (1988) The amylase gene-enzyme system of fishes. I. Developmental expression in the mosquitofish. J Exp Zool 245:24–32Google Scholar
  21. Yardley DG, Anderson WW, Schaffer HE (1977) Gene frequency changes at the α-amylase locus in experimental populations ofDrosophila pseudoobscura. Genetics 87:357–369Google Scholar
  22. Yardley DG, Martin MP (1982) The amylase system ofDrosophila pseudoobscura. I. Biochemical comparisons of the amylases. Comp Biochem Physiol 73B:243–249Google Scholar
  23. Yardley DG, Chernin MI (1984) The amylase system ofDrosophila. II. Biochemical comparisons of amylases fromD. pseudoobscura, D. persimilis, D. miranda andD. melanogaster. Comp Biochem Physiol 77B:107–113Google Scholar

Copyright information

© Springer-Verlag 1989

Authors and Affiliations

  • Darrell G. Yardley
    • 1
  1. 1.Department of Biological SciencesClemson UniversityClemsonUSA

Personalised recommendations