Einfluß niedriger SO₂-Konzentrationen auf die Aktivität einiger Glykosidasen der Assimilationsorgane verklonter Waldbäume

Abstract

6 Kerstin FlodinHiNTiKKA, V., 1970: Selective effect on wood-decomposing Hymenomycetes. Karstenia 11, 28-32. HiiTTERMANN, A.; GEBAUER, M.; VOLGER, C; ROSGER, C., 1977: Polymerisation und Abbau von Natrium-Ligninsulfonat durch Fomes annosus (Fr.) Cooke. Holzforschung31, 84-89. JOHANSSON, M.; HAGERBY, E., 1974: Influence of growth conditions, metabolic inhibitors and phenolic compounds on the ATP pool in Fomes annosus. Physiol. Plant. 32, 23-32. JOHANSSON, M.; POPOFF, T; THEANDER, O., 1976: Effect of spruce root constituents on extracellular enzymes of Fomes annosus. Physiol. Plant. 37, 275 -282. KAARIK, A., 1965: The identification of the mycelia of wood decay fungi by theu' oxidation reactions with phenolic compounds. Studia Forestalia Suecia. 31, 1-80. LiNDEBERG, G.; FAHRAEUS, G., 1952: Nature and formation of phenol oxidases in Polyporus zonatus mdP.versicolcr. Physio!. Plant. 5, 277-283. LoWRY, O.; RosEBROUGH, N. J.; FARR, L. A.; RANDALL, R. J., 1951: Protein measurement with the Folin phenol reagent. J. Biol. Chem. 193, 265-275. LYR, H., 1957: Ein neues Peroxidase-Bcstimmungsverfahren. Biochem. Z. 329, 91-96. -1958: Ober den Nachweis von Oxydasen und Peroxidasen bei hoheren Pilzen und die Bedeutung dieser Enzyme fur die Bavendammreaktion. Planta 50, 359-370. -1962: Enzyinatische Detoxifikation der Kernholztoxine. Flora 152, 570-579. POPOFF, T; THEANDER, O.; JOHANSSON, M., 1975: Changes in sapwood of roots of Norway spruce, attacked by Fomes annosus. 2. AbstractEffect of low SO2-concentrations on tbe activities of some glycosidases in the foliage of clonal forest trees. The aim was to find .in early indicator of latent: SO2 injuries in a beeeh and a spruce clone. After exposure to 0.0, 0.05, 0.1 and 0.2 ppm for several weeks in outdoor fumigation chambers, the activities of (i-glucosidase in the beech and ("i-galactosidase in the spruce clone and P-l,3-glucanase in both species were significantly raised. As the beech clone was very sensitive to SO2, an indication of latent injury could be ascertained only in the 0.05 ppm treatment where tbe rise of the f5-glucosidase activity appeared some days before necroses. Contrary to beecb, the spruce clone was tolerant to all SO2-treatments and the enxymatical changes could be used as early indicators of latent injuries.

Nutrient element and carbohydrate status of Norway spruce at Mt. Kleiner Feldberg in Taunus exposed to air pollution and soil acidification

“…When BUCHER-WALLIN et al (1979) exposed spruce cuttings for 6 weeks in November to 290 /xg SO2-m~' they found no changes in the activities of the enzymes a-galactosidase and a-mannosidase. On the stand Kleiner Feldberg both enzymes showed less activities in current-year needles of trees of damage class 3 than in those of damage class 0.…”

“…a-D-Galactosidase (EC 3.2.1.22) •was estimated at pH 5.5 according to BUCHER-WALLIN et al (1979) and enzyme activities were calculated for moles of nitrophenolate produced per second and grams of needle dry weight [kat (g DW)~'] taking a molar extinction coefficient of E4oo=2OO4 [1 (mol mm)"'].…”

“…Glycosidases were extracted using the method of BUCHER-WALLIN et al (1979). To extract dehydrogenases, transferases and isomerases a 100 mM Na-phosphate buffer of pH 7.5 was used which contained 0.5 % (w/v) Triton X-100 and 5 % (w/v) insoluble polyvinylpyrrolidone (WEIMAR and ROTHE 1987).…”

“…Enzyme activities were calculated for moles of H2O2 consumed per second and grams of needle dry weight [kat (g DW)~'] taking a molar extinction coefficient for tetraguajacol of E436=2550 [1 (mol mm)"']. a-D-Galactosidase (EC 3.2.1.22) •was estimated at pH 5.5 according to BUCHER-WALLIN et al (1979) and enzyme activities were calculated for moles of nitrophenolate produced per second and grams of needle dry weight [kat (g DW)~'] taking a molar extinction coefficient of E4oo=2OO4 [1 (mol mm)"'].…”

“…a-D-Mannosidase (EC 3.2.1.24) was estimated at pH 5.0 according to BUCHER-WALLIN et al (1979) and enzyme activities were calculated as described for alpha-D-galactosidase.…”