Premium
Temperature Response of Adenosine Triphosphatase of Bean Roots as Related to Growth Temperature and to Lipid Requirement of the Adenosine Triphosphatase
Author(s) -
KUIPER P. J. C.
Publication year - 1972
Publication title -
physiologia plantarum
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.351
H-Index - 146
eISSN - 1399-3054
pISSN - 0031-9317
DOI - 10.1111/j.1399-3054.1972.tb03568.x
Subject(s) - adenosine triphosphatase , phaseolus , atpase , microsome , acetone , chemistry , triphosphatase , biochemistry , pi , membrane , chromatography , enzyme , botany , horticulture , biology
The ATPase activity of the cell wall, mitochondrial and microsomal fractions of bean roots ( Phaseolus vulgaris ) shows non‐linear curves when plotted logarithmically against temperature, producing high Q 10 ‐values in the low temperature range and low Q 10 ‐values in the high temperature range. The Q 10 ‐valuc of supernatant ATPase is constant and low as well as the Q 10 ‐value of soluble ATPase liberated from membranes. Cell wall ATPase from bean roots adapted to a low temperature has a much smaller temperature response. Such roots contain a larger quantity of membrane‐bound ATPase and a smaller amount of soluble ATPase than roots adapted to a high temperature. Extraction of soluble ATPase with acetone reduces activity to practically zero, but activity could be partially restored by the addition of lipid. The temperature response of reconstituted phosphatidyl choline‐ATPase is inconsiderable. That of reconstituted sulfolipid‐ATPase is much larger. I am indebted to Bep Stuiver for skillful assistance with the experiments, to Ir. F. Kuiper and Mr. C. H. Vermeulen for help with the cultivation of the bean plants and to Prof. Dr. E. C. Wassink for reading the manuscript. Communication 292 of the Laboratory of Plant Physiological Research, Agricultural University, Wageningen, The Netherlands.