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Activity and activation state of ribulose-1,5-bisphosphate carboxylase of spruce trees with varying degrees of damage relative to the occurrence of novel forest decline

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Abstract

The aim was to determine whether a reduced carboxylation efficiency in needles of damaged spruce trees (Picea abies), is derived from a direct impairment of the ribulose-1,5-bisphosphate carboxylase (RuBP carboxylase) or there is an indirect inhibition of the RuBP carboxylase. In 1985, 1986 and 1987 measurements of RuBP carboxylase activity were carried out at three locations. Trees of different ages and degrees of damage were examined. RuBP carboxylase was assayed using both a rapid extraction method to determine the initial activity and an in vitro test after total activation to determine the total activity. The activation state was calculated as the ratio of initial activity to total activity.

Within three vegetation periods the total activity in needles of damaged and apparently healthy or slightly damaged spruce trees indicated no definite difference in the annual average. On the other hand, in damaged needles a continued decline of the actual activation of RuBP carboxylase was established. The observation of continued depression of the activation state of the enzyme in needles of damaged spruce trees can possibly be due to a reduced photosynthetic electron transport rate.

The measurements of the soluble protein content indicate a tendency to increased amounts in the needles of damaged trees. In accordance, a considerable increase of the activity of some enzymes like glutamine synthethase, phosphoenol-pyruvate carboxylase, and catalase could be noticed. However, there is no clear connection between the RuBP carboxylase and the content of soluble proteins.

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Abbreviations

chl:

chlorophyll a+b, dw-dry weight, i.a-initial activity

P-700:

reaction center of photosystem I

PVP:

polyvinylpyrrolidone 25

RuBP:

ribulose-1,5-bisphosphate

RuBPCase:

ribulose-1,5-bisphosphate carboxylase

t.a.:

total activity

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Authors and Affiliations

  1. Institut für Allgemeine Botanik, Johannes Gutenberg-Universität Mainz, Saarstraße 21, D-6500, Mainz, F.R.G.

    Ursula Schmieden-Kompalla, Ursula Hartmann, Sabine Korthals & Aloysius Wild

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  1. Ursula Schmieden-Kompalla
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  2. Ursula Hartmann
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  3. Sabine Korthals
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  4. Aloysius Wild
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Schmieden-Kompalla, U., Hartmann, U., Korthals, S. et al. Activity and activation state of ribulose-1,5-bisphosphate carboxylase of spruce trees with varying degrees of damage relative to the occurrence of novel forest decline. Photosynth Res 21, 161–169 (1989). https://doi.org/10.1007/BF00037180

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  • DOI: https://doi.org/10.1007/BF00037180

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