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Microcystis, a genus of potentially harmful cyanobacteria, is known to proliferate in stratified freshwaters due to its capability to change cell density and regulate buoyancy. In this study, a trajectory model was developed to simulate the cell density change and spatial distribution of Microcystis cells with nonuniform colony sizes. Simulations showed that larger colonies migrate to the near-surface water layer during the night to effectively capture irradiation and become heavy enough to sink during daytime. Smaller-sized colonies instead took a longer time to get to the surface. Simulation of the diurnally varying Microcystis population profile matched the observed pattern in the field when the radii of the multisized colonies were in a beta distribution. This modeling approach is able to take into account the history of cells by keeping track of their positions and properties, such as cell density and the sizes of colonies. It also serves as the basis for further developmental modeling of phytoplanktons that are forming colonies and changing buoyancy.

Bioaerosols generated during livestock and poultry production are significant occupational hazards. This study investigates the characteristics of bioaerosols released from animal feces. Fresh feces from pigs and chickens were obtained and tested in a controlled-environment facility. Airborne viable (culturable) bacteria and fungi were sampled hourly for 48 hr. The predominant species were identified via polymerase chain reaction analysis. The number of bacterial colonies released from chicken feces increased gradually, peaked at approximately 20 hr, and remained relatively constant to test end; however, the bacterial colonies released from swine feces did not increase significantly. The chicken feces released significantly (P0.05) more bacterial aerosols than swine feces over 40 hr, by approximately 1 order of magnitude. However, the difference in total fungal aerosols released from the two feces types was relatively small (30-40%) and insignificant (P0.05). Aerosols sized between approximately 0.65 and 1.1 microm were predominant for bacteria, whereas aerosols sized between approximately 2.1 and 3.3 microm prevailed for fungi. Genera Stenotrophomonas were the predominant bacterial aerosols, whereas Cladosporium and Acremonium accounted for the greatest amounts of fungi from chicken and swine feces, respectively. More than 1000 culturable bacterial colonies can be released from 1 g of chicken feces per hour, and approximately 80% of these bioaerosols are respirable. Most bacterial aerosols released from swine and chicken feces were opportunistic human pathogens; thus, the significance of their presence warrants further investigations.

Human mitochondrial NAD(P)+-dependent malic enzyme is inhibited by ATP. The X-ray crystal structures have revealed that two ATP molecules occupy both the active and exo site of the enzyme, suggesting that ATP might act as an allosteric inhibitor of the enzyme. However, mutagenesis studies and kinetic evidences indicated that the catalytic activity of the enzyme is inhibited by ATP through a competitive inhibition mechanism in the active site and not in the exo site. Three amino acid residues, Arg165, Asn259, and Glu314, which are hydrogen-bonded with NAD+ or ATP, are chosen to characterize their possible roles on the inhibitory effect of ATP for the enzyme. Our kinetic data clearly demonstrate that Arg165 is essential for catalysis. The R165A enzyme had very low enzyme activity, and it was only slightly inhibited by ATP and not activated by fumarate. The values of K(m,NAD) and K(i,ATP) to both NAD+ and malate were elevated. Elimination of the guanidino side chain of R165 made the enzyme defective on the binding of NAD+ and ATP, and it caused the charge imbalance in the active site. These effects possibly caused the enzyme to malfunction on its catalytic power. The N259A enzyme was less inhibited by ATP but could be fully activated by fumarate at a similar extent compared with the wild-type enzyme. For the N259A enzyme, the value of K(i,ATP) to NAD+ but not to malate was elevated, indicating that the hydrogen bonding between ATP and the amide side chain of this residue is important for the binding stability of ATP. Removal of this side chain did not cause any harmful effect on the fumarate-induced activation of the enzyme. The E314A enzyme, however, was severely inhibited by ATP and only slightly activated by fumarate. The values of K(m,malate), K(m,NAD), and K(i,ATP) to both NAD+ and malate for E314A were reduced to about 2-7-folds compared with those of the wild-type enzyme. It can be concluded that mutation of Glu314 to Ala eliminated the repulsive effects between Glu314 and malate, NAD+, or ATP, and thus the binding affinities of malate, NAD+, and ATP in the active site of the enzyme were enhanced.