The present study was performed to evaluate the potential of microbial phytase and cholecalciferol (D3) for improving the utilization of phytate P and Ca and the influence of the Car:total (t) P ratio in a corn-soybean meal diet fed to broilers from hatch to 21 d of age. A 4 x 4 x 2 factorial arrangement of treatments was used: 1.1, 1.4, 1.7, and 2.0:1 Ca:tP ratio; 0, 300, 600, and 900 U of phytase/kg of diet; and 66 and 660 micrograms of D3/kg of diet. Another four treatments were included: the four Ca:tP ratios with 6,600 micrograms of D3 addition, but without phytase. Added phytase linearly increased (P < 0.001) BW gain, feed intake, toe ash content, and P and Ca retention; these measurements were negatively influenced by widening the dietary Ca:tP ratio, and synergetically improved by addition of D3. Increasing the Ca:tP ratio decreased (P < 0.001) all measurements in the presence or absence of supplemental phytase and D3. Dietary Ca:tP ratios between 1.1:1 to 1.4:1 appears critical to the efficient use of supplemental phytase and D3 for improving the utilization of phytate P and Ca. The addition of D3 in corn-soybean meal diets indicated a potential for improving the utilization of phytate P and Ca by increasing Ca and P retention by about 5 to 12% in birds, which led to an increase in toe ash content (P < 0.03). The enhanced phytate P utilization (P < 0.001) was also observed during assay of the phytase activity in the mixed diets with an addition of D3 and without added phytase. In summary, the findings of this study suggested that phytase, D3, and Ca:tP are important factors in degrading phytate and improving phytate P and Ca utilization in broilers.
We present an experimental study encompassing synthesis and characterization of fully conjugated tri(perylene bisimides) (triPBIs), having 19 six-membered carbon rings in the core and six imide groups at the edges. Two structural isomers of triPBIs resulting from the two probable coupling positions were successfully separated by HPLC. To assist the identification of the two structural isomers, quantum-chemical calculations of electronic structure, NMR, and optical spectra were carried out. Calculations predict stable helical and nonhelical configurations for both triPBIs isomers and allow the assignment of triPBIs 6 unequivocally to the most bathochromically shifted absorption spectrum. Increasing the number of PBI units in oligo-PBIs leads to an expansion of the pi system, in turn associated with a reduction of the transport and optical band gaps, and a remarkable increase in electron affinities, which make oligo-PBIs promising n-type functional components in optoelectronic devices.
Asymmetric division of Drosophila neuroblasts (NBs) and the Caenorhabditis elegans zygote uses polarity cues provided by the Par proteins, as well as heterotrimeric G-protein-signalling that is activated by a receptor-independent mechanism mediated by GoLoco/GPR motif proteins. Another key component of this non-canonical G-protein activation mechanism is a non-receptor guanine nucleotide-exchange factor (GEF) for Galpha, RIC-8, which has recently been characterized in C. elegans and in mammals. We show here that the Drosophila Ric-8 homologue is required for asymmetric division of both NBs and pl cells. Ric-8 is necessary for membrane targeting of Galphai, Pins and Gbeta13F, presumably by regulating multiple Galpha subunit(s). Ric-8 forms an in vivo complex with Galphai and interacts preferentially with GDP-Galphai, which is consistent with Ric-8 acting as a GEF for Galphai. Comparisons of the phenotypes of Galphai, Ric-8, Gbeta13Fsingle and Ric-8;Gbeta13F double loss-of-function mutants indicate that, in NBs, Ric-8 positively regulates Gai activity. In addition, Gbetagamma acts to restrict Galphai (and GoLoco proteins) to the apical cortex, where Galphai (and Pins) can mediate asymmetric spindle geometry.
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