Damage to living trees contributes to almost half of the biomass losses in tropical forests

Accurate estimates of forest biomass stocks and fluxes are needed to quantify global carbon budgets and assess the response of forests to climate change. However, most forest inventories consider tree mortality as the only aboveground biomass (AGB) loss without accounting for losses via damage to living trees: branchfall, trunk breakage, and wood decay. Here, we use ~151,000 annual records of tree survival and structural completeness to compare AGB loss via damage to living trees to total AGB loss (mortality + damage) in seven tropical forests widely distributed across environmental conditions. We find that 42% (3.62 Mg ha⁻¹ year⁻¹; 95% confidence interval [CI] 2.36–5.25) of total AGB loss (8.72 Mg ha⁻¹ year⁻¹; CI 5.57–12.86) is due to damage to living trees. Total AGB loss was highly variable among forests, but these differences were mainly caused by site variability in damage-related AGB losses rather than by mortality-related AGB losses. We show that conventional forest inventories overestimate stand-level AGB stocks by 4% (1%–17% range across forests) because assume structurally complete trees, underestimate total AGB loss by 29% (6%–57% range across forests) due to overlooked damage-related AGB losses, and overestimate AGB loss via mortality by 22% (7%–80% range across forests) because of the assumption that trees are undamaged before dying. Our results indicate that forest carbon fluxes are higher than previously thought. Damage on living trees is an underappreciated component of the forest carbon cycle that is likely to become even more important as the frequency and severity of forest disturbances increase.     

Effect of different doses of chromium picolinate on protein metabolism in infant rats.

This 12-day study was conducted to evaluate the effects of three different levels of dietary chromium (100, 200, and 500 microg/day) in the form of chromium picolinate (CrPic) on growth and protein use in weaned rats. No significant effect of CrPic on body weight gain, food intake, or food conversion rate was observed. Elevated doses of CrPic seemed to increase muscle mass, either by stimulating protein anabolism by activation of insulin by chromium or by lowering protein degradation. However, these effects had no repercussions on overall growth, suggesting that any anabolic effect of chromium due to the action of insulin was probably marginal.     

The pattern of testosterone replacement influences the recovery of the stimulatory effect of clonidine on growth hormone (GH) secretion in orchidectomized rats

It has previously been described that the growth hormone (GH) releasing effect of clonidine (CLO), an agonist of ₂-adrenoreceptors, disappears after orchidectomy and is restored by testosterone replacement when started immediately after orchidectomy. In the present experiments, the effects of CLO on GH release was analysed in long-term (LTO; 12 weeks) and short-term (STO; 2 weeks) orchidectomized rats. In the first experiment, LTO males were implanted with silastic capsules containing testosterone 10 weeks after orchidectomy and killed 2 weeks later, 15 min after injection of CLO (150 μg/kg) or vehicle. In the second experiment, adult males were implanted with testosterone at the moment of orchidectomy and decapitated 2 or 12 weeks later, 15 min after vehicle or CLO administration. In addition, in order to evaluate the effects of orchidectomy and androgen replacement on ₂ agonists GH release further, prepubertal males (21-days-old) implanted with testosterone or 5--androstane-3-, 17β diol (-diol) at the moment of orchidectomy were killed 2 weeks later, 15 min after ketamine-xylazine (an ₂ agonist) administration. Finally, 10-day-old males (orchidectomized 72 h before) were decapitated 15 min after CLO or vehicle administration. Our results show that: (a) LTO and STO abolished the stimulatory effect of clonidine on GH secretion; (b) orchidectomy also abolished the stimulatory effect of clonidine in neonatal rats and that of xylazine in prepubertal males; (c) testosterone implanted at the moment of orchidectomy prevented the loss of the CLO effect in LTO and STO, but testosterone-delayed administration in LTO was unable to restore the effectiveness of CLO inducing GH release. We conclude that orchidectomy at all ages tested abolishes GH secretion induced by ₂ agonists, which suggests that the functionality of -adrenergic receptors involved in the control of GH secretion is critically dependent on a permanent exposure to testosterone in males.     

Purification and partial characterization of an acidic ribosomal protein kinase from maize

Phosphorylation and dephosphorylation of ribosomal proteins have been suggested to participate in the regulation of protein synthesis in eukaryotic organisms. The present research focuses on the purification and partial characterization of a protein kinase from maize ribosomes that specifically phosphorylates acidic ribosomal proteins. Ribosomes purified from maize axes were used as the enzyme source. Purification of ribosomes was performed by centrifugation through a 0.5 M sucrose, 0.8 M KCl cushion. A protein kinase activity present in this fraction was released by extraction with 1.5 M KCl and further purified by diethylaminoethyl cellulose column chromatography. A peak containing protein kinase activity was eluted around 400 m M KCl. Analysis of this fraction by sodium dodecyl sulfate-polyacrylamide gel electrophoresis showed one band of 38 kDa molecular mass, which cross-reacted in a western blot with antibodies raised against proteins from the large ribosomal subunit. This enzyme specifically phosphorylates one of the acidic ribosomal proteins (P₂). Its activity is inhibited by Ca²⁺ and Zn²⁺ and is activated by Mg²⁺, polylysine and spermine. The relevance of this protein kinase in reinitiating the protein synthesis process during germination is discussed.     

Amino acid sequence of the minor isomorph of the crustacean hyperglycemic hormone (CHH-II) of the Mexican crayfish Procambarus bouvieri (Ortmann): Presence of a d-amino acid

The primary structure of the neurohormone crustacean hyperglycemic hormone (CHH-II) was determined by means of enzymatic digestions, manual Edman degradation, and mass spectrometry. CHH-II is a 72 residue peptide (molecular mass 8388 Da), with six cysteines forming three disulfide bridges that connect residues 7–43, 23–39, and 26–52. The peptide has blocked N- and C-termini, and lacks tryptophan, histidine, and methionine. The CHH-I and CHH-II of Procambarus bouvieri have identical sequences and elicit levels of hyperglycemia that are not distinguishable. The difference between the two isomorphs consists in a posttranslational modification of a l-Phe in CHH-I to a d-Phe in CHH-II at the third position from the N-terminus.     

Detection and minimization of H-phosphonate side reaction during phosphopeptide synthesis by a post-assembly global phosphorylation strategy

Summary In the course of solid-phase synthesis of phosphopeptides by a post-assembly global phosphorylation strategy, the corresponding H-phosphonate peptides form as byproducts. We describe model studies to investigate this side reaction as a function of reaction conditions, and use this information to develop conditions that minimize the problem, i.e., use of dibenzyl N,N-di-isopropyl phosphoramidite for phosphitylation, followed immediately by oxidation with anhydrous tert-butyl hydroperoxide in dry tetrahydrofuran under argon, and final acidolytic cleavage.This work was taken in part from the Ph.D. Theses of E.A. Ottinger (1994) and Q. Xu (1996), University of Minnesota, Minneapolis, MN, U.S.A. Preliminary presentations of portions of this work were made at the Twenty-Second European Peptide Symposium, Interlaken, Switzerland, September 13–19, 1992, see Ref. 1, at the 14th American Peptide Symposium, Columbus, OH, U.S.A., June 18–23, 1995, and at the Fourth International Symposium on Solid Phase Synthesis & Combinatorial Chemical Libraries, Edinburgh, Scotland, U.K., September 12–16, 1995, see Ref. 2. The title side reaction was first discussed for tyrosine (see Refs 1 and 3), but all of the mechanism studies discussed herein are for serine and threonine.Amino acid symbols denote the l-configuration, and abbreviations for amino acids and peptides follow rules of the IUPAC-IUB Commission of Biochemical Nomenclature [J. Biol. Chem., 247 (1972) 977].     

Direct transfer of molybdopterin cofactor to aponitrate reductase from a carrier protein in Chlamydomonas reinhardtii.

A Chlamydomonas reinhardtii molybdenum cofactor (MoCo)-carrier protein (CP), capable of reconstituting nitrate reductase activity with apoprotein from the Neurospora crassa mutant nit-1, was subjected to experiments of diffusion through a dialysis membrane and gel filtration. CP bonded firmly MoCo and did not release it efficiently unless aponitrate reductase was present in the incubation mixture. Stability of MoCo bound to CP against air and heat was very similar to that of free-MoCo released from milk xanthine oxidase. Our data strongly suggest that MoCo is directly transferred from CP to aponitrate reductase to form an active enzyme.     

Oxygen regulation of L-1,2-propanediol oxidoreductase activity in Escherichia coli.

Regardless of the respiratory conditions of the culture, Escherichia coli synthesizes an active propanediol oxidoreductase. Under anaerobic conditions, the enzyme remained fully active and accomplished its physiological role, while under aerobic conditions, it was inactivated in a process that did not depend on protein synthesis or on the presence of a carbon source.