Life in the Open Ocean. Joseph J. Torres

Читать онлайн книгу.

Life in the Open Ocean - Joseph J. Torres


Скачать книгу
solution to synthesize larger quantities of an inefficient enzyme to deal with the cold.

      Compensation via Changes in Enzyme Quality – Isozymes, Allozymes, and Temperature Adaptation

      Metabolic adaptation to temperature in eurythermal species may involve a change in the quantity or concentration of enzyme, as observed above in Sidell et al.’s goldfishes, or to actually change the enzyme to one that functions better at the new temperature. For those species that are genetically equipped to do so, the change in enzyme may be the result of an enzyme produced by a different gene locus (a different isozyme) or by a different allele of the same gene locus (a different allozyme).

Schematic illustration of changes in enzyme activity as a function of time after changes in acclimation temperature.

      Source: Sidell et al. (1973), figures 1 and 2 (p. 210). Reproduced with the permission of Springer‐Verlag.

Schematic illustration of the effect of temperature on the Km of acetylcholine for acetylcholinesterase enzymes of four species of fish acclimated to different environmentally relevant temperatures.

      Source: Hochachka and Somero (1973), figure 7‐14 (p. 231). Reproduced with the permission of Saunders Publishing.

      Diploid species have two copies of each gene, the two alleles, of which one is normally dominant. A study by Place and Powers (1979) observed the expression of two allozymes for LDH B in the killifish Fundulus heteroclitus. LDH B is the type normally found in the heart, as opposed to LDH A normally found in skeletal muscle. Fundulus is a widely distributed species along the east coast of the USA, and the Place and Powers study used specimens obtained from Maine to Florida. They found that the two types of LDH B had different efficiencies with respect to temperature, one more efficient in the cold and the other more efficient at warm temperatures. The presence of the different allozymes scaled with the environmental cline in temperature along the eastern US seaboard.

      A good example of a more typical situation is provided in a study by Graves and Somero (1982) of Pacific barracudas, congeneric pelagic fishes with similar ecologies differing in habitat temperature by only a few degrees: 6–8 °C. The four congeneric species were Sphyraena argentea and S. idiastes, both cold‐temperate species, S. lucasana, a warm‐temperate species, and S. ensis, a tropical‐subtropical species. The study used purified enzymes of LDH A to evaluate the effect of temperature on the Km (Michaelis constant) and the Kcat of the four species. Kcat is the catalytic efficiency of an enzyme, specifically the rate at which substrate is converted to product per unit time, per active site. Thus, activity of an enzyme = (Kcat) × the concentration of the enzyme.

      The electrophoretic properties of the four species were separated into three patterns, with the two cold‐temperate species (S. argentea and S. idiastes) showing identical mobility. S. lucasana and S. ensis (T‐ST) were different from one another, and both were different from S. argentea and S. idiastes. The electrophoretic study suggested three different enzyme structures, one for the two cold‐temperate species, and one each for the warm‐temperate and tropical‐subtropical species. A look at the kinetic characteristics of the enzymes showed that they differed in those properties as well.

Schematic illustration of the effect of temperature on apparent Michaelis constant (Km) of pyruvate for the M4-LDH's of three eastern Pacific barracudas.
Скачать книгу