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Fine-root turnover rates of European forests revisited: an analysis of data from sequential coring and ingrowth cores
Background and Aims
Forest trees directly contribute to carbon cycling in forest soils through the turnover of their fine roots. In this study we aimed to calculate root turnover rates of common European forest tree species and to compare them with most frequently published values.
Methods
We compiled available European data and applied various turnover rate calculation methods to the resulting database. We used Decision Matrix and Maximum-Minimum formula as suggested in the literature.
Results
Mean turnover rates obtained by the combination of sequential coring and Decision Matrix were 0.86 yr−1 for Fagus sylvatica and 0.88 yr−1 for Picea abies when maximum biomass data were used for the calculation, and 1.11 yr−1 for both species when mean biomass data were used. Using mean biomass rather than maximum resulted in about 30 % higher values of root turnover. Using the Decision Matrix to calculate turnover rate doubled the rates when compared to the Maximum-Minimum formula. The Decision Matrix, however, makes use of more input information than the Maximum-Minimum formula.
Conclusions
We propose that calculations using the Decision Matrix with mean biomass give the most reliable estimates of root turnover rates in European forests and should preferentially be used in models and C reporting
Conserved cystatin segments as models for designing specific substrates and inhibitors of cysteine proteinases
Peptide segments derived from consensus sequences of the inhibitory site of cystatins, the natural inhibitors of cysteine proteinases, were used to develop new substrates and inhibitors of papain and rat liver cathepsins B, H, and L. Papain hydrolyzed Abz-QVVAGA-EDDnp and Abz-LVGGA-EDDnp at about the same rate, with specificity constants in the 10(7) M(-1) sec(-1) range; cathepsin L also hydrolyzes both substrates with specificity constants in the 10(5) M(-1) sec(-1) range due to lower k(cat) values, with the K-m's being identical to those with papain. Only Abz-LVGGA-EDDnp was rapidly hydrolyzed by cathepsin B, and to a lesser extent by cathepsin H. Peptide substrates that alternate these two building blocks (LVGGQVVAGAPWK and QVVAGALVGGAPWK) discriminate the activities of cathepsins B and L and papain. Cathepsin L was highly selective for cleavage at the G-G bond of the LVGG fragment in both peptides. Papain and cathepsin B cleaved either the LVGG fragment or the QVVAG fragment, depending an their position within the peptide. While papain was more specific for the segment located C-terminally, cathepsin B was specific for that in N-terminal position. Peptidyl diazomethylketone inhibitors based an these two sequences also reacted differently with papain and cathepsins. GlcA-QVVA-CHN, was a potent inhibitor of papain and reacted with papain 60 times more rapidly (k(+0) = 1,100,000 M(-1) sec(-1)) than with cathepsin L, and 220 times more rapidly than with cathepsin B. Cathepsins B and L were preferentially inhibited by Z-RLVG-CHN2. Thus cystatin-derived peptides provide a valuable framework for designing sensitive, selective substrates and inhibitors of cysteine proteinases.UNIV TOURS,FAC MED,CNRS URA 1334,LAB ENZYMOL & CHIM PROT,F-37032 TOURS,FRANCEESCOLA PAULISTA MED,INFAR,DEPT BIOFIS,BR-04044020 São Paulo,BRAZILCNRS,CTR BIOPHYS MOLEC,LAB BIOCHIM GLYCOCONJUGUES & LECTINES ENDOGENES,F-45071 ORLEANS 2,FRANCEESCOLA PAULISTA MED,INFAR,DEPT BIOFIS,BR-04044020 São Paulo,BRAZILWeb of Scienc