THERMAL SENSITIVITIES OF MALATE DEHYDROGENASE ISOZYMES IN TYPHA

Publisher Website
Google Scholar
Abstract
Two species of cattail. Typha latifolia L. and T. domingensis Pers., occur naturally along the shoreline of Par Pond, an 1,128 ha impoundment subjected to intermittent thermal stress at the Savannah River Plant in South Carolina. T. domingensis is not tolerant of the stresses imposed at the hottest section of this lake. Typha latifolia is established throughout the lake but at the hottest section displays an altered morphology compared with stands from ambient areas. Both T. latifolia and T. domingensis are electrophoretically monomorphic, and no variation in isozyme expression in ten enzyme systems was recorded in populations from Par Pond. The malate dehydrogenase (MDH) isozyme patterns for T. latifolia and T. domingensis are identical, but their thermal sensitivities differ sharply. All six major T. domingensis MDH isozymes are denatured by heating at 50 C; whereas, T. latifolia has three isozymes which are stable at 50 C and three isozymes which are denatured at this temperature. Tests of thermal stability are more useful than measurements of electrophoretic mobility in detecting enzyme differences and a possible biochemical basis for differences in thermal tolerance in these natural populations.
Funding Information
  • U.S.-E.R.D.A. (EY-76-C-09-0819)