Thermostability of acid phosphatase inSelinum vaginatum Clarke andAcer caesium Wall. grown at low and high altitudes
Authors:
- 1 November 1986
- journal article
- conference paper
- Published by Institute of Experimental Botany in Biologia plantarum
- Vol. 28 (6) , 465-469
Abstract
Acid phosphatase isolated from low altitude grown plants of two high altitude plant species,Selinum vaginatum Clarke andAcer caesium Wall, displayed higher thermostability than that from plants of the same species grown at high altitude. The isozyme composition, however, remained unchanged inSelinum vaginatum. InA. caesium, one of four isozymes, was thermolabile in the samples from high altitude and was lost after 10 min heating of the extracts at 60 °c. In the samples from low altitude, this isozyme was not detected and a band with slightly lower Rf value was present which was thermostable. The described changes in the thermal properties of acid phosphatase reflect an adaptive step towards high temperature acclimation at low altitude.Keywords
This publication has 9 references indexed in Scilit:
- Genotypic temperature adaptations of cellular functions and proteins in two Zostera speciesOecologia, 1981
- Effect of heat-hardening on thermostability of acid phosphatase from wheat leavesJournal of Thermal Biology, 1979
- Cells, Molecules and Temperature1977
- Changes in Microsomal Enzymes and Phospholipid during Dehardening in Stem Bark of Black LocustPlant Physiology, 1976
- Resistance of some proteins of Pisum sativum L. leaves after heat hardening to elevated temperature, proteolysis and shifts in pHJournal of Thermal Biology, 1975
- The responsive increase in thermostability of plant cellsProtoplasma, 1970
- Isoenzyme Polymorphism in Flowering Plants III Gel Electrophoretic Methods and ApplicationsPhysiologia Plantarum, 1968
- The effect of heat hardening on the heat resistance of some enzymes from plant leavesPlanta, 1968
- DISC ELECTROPHORESIS – II METHOD AND APPLICATION TO HUMAN SERUM PROTEINS*Annals of the New York Academy of Sciences, 1964