Physiological effects of an allozyme polymorphism: glutamate-pyruvate transaminase and response to hyperosmotic stress in the copepod Tigriopus californicus.
In order to regulate cell volume during hyperosmotic stress, the intertidal copepod Tigriopus californicus, like other aquatic crustaceans, rapidly accumulates high levels of intracellular alanine, proline, and glycine. Glutamate-pyruvate transaminase (GPT; EC 2.6.1.2), which catalyzes the final step of alanine synthesis, is genetically polymorphic in T. californicus populations at Santa Cruz, California. Spectrophotometric studies of homogenates derived from a homozygous isofemale line of each of the two common GPT alleles indicated that the GPTF allozyme has a significantly higher specific activity than the GPTS allozyme. Under conditions of hyperosmotic stress, individual adult copepods of GPTF and GPTF/S genotypes accumulated alanine, but not glycine or proline, more rapidly than GPTS homozygotes. When young larvae were subjected to the same hyperosmotic conditions, GPTS larvae suffered a significantly higher mortality than GPTF or GPTF/S larvae. These results suggest that the biochemical differences among GPT allozymes result in specific physiological variation among GPT genotypes and that this physiological variation is manifested in differential genotypic survivorships under some naturally occurring environmental conditions.
D000410:Alanine Transaminase / Q000235:genetics*; D000818:Animals; D003445:Crustacea / Q000235:genetics / Q000502:physiology*; D005796:Genes; D007527:Isoenzymes / Q000235:genetics*; D009997:Osmotic Pressure; D011110:Polymorphism, Genetic
D007527:Isoenzymes; D000410:Alanine Transaminase