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Ribulose‐l,5‐bisphosphate carboxylase activity and influence of air pollution in spruce
Author(s) -
Weidner Manfred,
Kraus Monika
Publication year - 1987
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.1399-3054.1987.tb04322.x
Subject(s) - picea abies , pyruvate carboxylase , ribulose 1,5 bisphosphate , rubisco , botany , karst , chemistry , chlorophyll , extraction (chemistry) , photosynthesis , enzyme , enzyme assay , horticulture , biology , biochemistry , chromatography , paleontology
Methods were established, which render possible a simultaneous determination of ri‐bulose‐l,5‐bisphosphate (RuBP) carboxylase (EC 4.1.1.39) activity and chlorophyll content of Norway spruce (Picea abies Karst.) needles from a detergent‐containing aqueous crude extract. Spruce RuBP carboxylase was tentatively characterized with regard to kinetic properties. Recovery experiments employing purified wheat RuBP carboxylase proved quantitative extraction of the enzyme from spruce foliage. Five timber stands consisting of 35–62 years old spruce, two of which exhibited the typical symptoms of recent spruce decline, were compared. For the needle generations 1 to 4 the enzyme activities as well as chlorophyll and protein concentrations were determined. The results do not indicate an involvement of RuBP carboxylase in spruce decline.