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Forest dynamics need to be considered when estimating the global carbon budget. The alteration of forest structure and function under a changing climate and expanding human activity could lead to a reduction of forest canopy cover and a spread of lower-biomass ecosystems in warm and dry regions. A non-structural carbohydrate (NSC) acts as a storage buffer between carbon supplied by assimilation and carbon consumed by, inter alia, respiration, reproduction, and pests. Estimation of NSC concentrations in a tree is very important for accurate projection of future forest dynamics. We developed a new NSC module for incorporation into a spatially explicit individual-based dynamic global vegetation model (SEIB-DGVM) to validate the simulated NSC dynamics with observations. NSC pools were simulated in three plant organs: leaves, trunk, and roots. The seasonal dynamics of the NSCs varied among plant species, and the sizes of the NSC pools inferred from observations differed between the boreal, temperate, and tropical climates. The NSC models were therefore validated for each of the three climatic regions at both point and global scales to assess the performance of the models. The modeled NSCs showed good agreement in seasonality with the observed NSCs at four sites – Canada (boreal), Austria and Switzerland (temperate), and Panama (tropical) – and in mean values for three climate zones derived from the global NSC dataset. The SEIB-DGVM-NSC version 1.0 is expected to enable simulation of biome shifts caused by the changes in NSC dynamics worldwide. These dynamics will contribute to changes in not only the global carbon cycle but also in forest structure and demography at a global scale.

The ''esterase'' activity of hormone-sensitive lipase (HSL) was studied using water-soluble p-nitrophenyl butyrate (PNPB) as a substrate. Bovine adipose tissue HSL was purified to near homogeneity by precipitation at pH 5.0, followed by chromatography on DEAE-cellulose, phenyl-Sepharose, and high performance ion-exchange columns on Mono Q and Mono S. The purified preparation hydrolyzed emulsified triolein and cholesteryl oleate (CO), and water-soluble PNPB. In the two last steps of purification, the elution profile of the CO-hydrolyzing activity coincided with that of PNPB-hydrolyzing activity. The HSL was adsorbed to heparin-Sepharose and the CO- and PNPB-hydrolyzing activities were eluted together in the same peak. Diisopropylfluorophosphate (DFP) strongly inhibited the HSL activities and the inhibition profiles of the triolein-; CO-, and PNPB-hydrolyzing activities were essentially identical. Only one polypeptide of Mr 84,000 in partial purified HSL fraction was labeled by affinity labeling with [3H]DFP. On digestion of the enzyme with trypsin, the triolein- and CO-hydrolyzing activities were lost more rapidly than the PNPB-hydrolyzing activity. Phosphorylation increased the triolein-hydrolyzing activity to 40% more than that of the control, but did not affect the CO- and PNPB-hydrolyzing activities.