Maize plant inbred lines, one Al-sensitive (B-73) and two Al-tolerant (F-2 and L-2039), were grown hydroponically in the presence of 200 µM Al. After 13 d of growth, root and shoot lengths, photosystem 2 (PS2) activity, chlorophyll (Chl) content, 5-aminolevulinic acid (5-ALA) synthesis rate, chlorophyllase (Chlase) activity, and N, Mg, Fe, and Mn contents in leaves were determined. PS2 activity and Chl content were most severely affected by Al in B-73, but F-2 was almost unaffected. This was in accordance with Al-accumulation in the plants. The observed changes in B-73 coincided with 5-ALA synthesis inhibition, Chlase activation, and leaf deprivation of Fe and Mg. In Al-treated L-2039 plants, the leaf Mg and Mn contents were decreased. Also, an excessive Chlase activation was found in Al-treated L-2039, without a substantial Chl loss. This may indicate the activation of different enzyme pools in tolerant and sensitive genotypes under low-stress conditions. and N. Mihailovic, G. Drazic, Z. Vucinic.
In Ochroma pyramidale (Cav. ex Lam.) Urb., photon-saturated photosynthetic capacity (PNmax) was 13 μmol(CO2) m-2 s-1. Average stomatal conductance (gs) and water-use efficiency (WUE) were greater at high irradiance, about 260 mmol(H2O) m-2 s-1 and 2.15 g(C) kg-1(H2O), respectively. In the dark, gs values were about 30% of maximum gs. Leaf nutrient contents on a leaf area basis were 131, 15, 36, 21, and 12 mmol m-2 for N, P, K, Ca, and Mg, respectively. Ochroma also accumulated a greater amount of soluble saccharides than starch, 128 versus 90 g kg-1 (DM). The availability of N and Mg, but not P, Ca, or K, may limit photosynthetic rates of Ochroma in this site. and R. A. Marenco, J. F. de C. Gonçalves, G. Vieira.
Intact chloroplasts were isolated from dark-senescing primary barley (Hordeum vulgare L.) leaves in order to study selective ribulose-1,5-bisphosphate carboxylase/oxygenase (RuBPCO) degradation by the stromal and membrane fractions. RuBPCO specific degradation was estimated and characterised applying sensitive avidin-biotin ELISA method with non-modified or oxidatively modified biotinylated RuBPCO (BR) as substrates. Distinct proteolytic activities were detected. They differed in ATP and divalent metal ion dependence, protease inhibitory profile, and dynamics in the time-course of dark-induced senescence. The results supported involvement of ATP- and metal ion-dependent serine type proteolytic activity against non-modified BR early in induced senescence and appearance of ATP-independent activity at later stage. Active oxygen-modified BR was degraded by ATP-independent serine-type protease probably containing essential SH-groups and requiring divalent metal ions. and L. Simova-Stoilova, K. Demirevska-Kepova, Z. Stoyanova.
Incubation of maize NADP-malic enzyme with tetranitromethane (TNM) resulted in a total loss of enzyme activity. The loss of enzyme activity was not observed at pH 6.3 but at pH 8.0. NADP-malic enzyme was inactivated to almost 90 % by incubation with an 80-fold molar excess of TNM for 5 min at 30 °C. The substrate malate or Mg2+ alone gave no protection, while NADP provided considerable protection. NADP in the presence of malate and Mg2+ totally protected the enzyme activity, suggesting that tyrosine residue may be located at or near the active site of maize NADP-malic enzyme. The spectral analysis of the modified enzyme indicated that modification of at least one tyrosine residue per subunit resulted in complete loss of the enzyme activity. The fluorescence study of unmodified and modified enzymes postulated that essential tyrosine residue at maize NADP-malic enzyme is possibly involved in malate binding. and S. R. Rao, B. G. Kamath, A. S. Bhagwat.