Quotient graphs for power graphs

In a previous paper of the first author a procedure was developed for counting the components of a graph through the knowledge of the components of its quotient graphs. We apply here that procedure to the proper power graph $\mathcal{P}_0(G)$ of a finite group $G$, finding a formula for the number $c(\mathcal{P}_0(G))$ of its components which is particularly illuminative when $G\leq S_n$ is a fusion controlled permutation group. We make use of the proper quotient power graph $\widetilde{\mathcal{P}}_0(G)$, the proper order graph $\mathcal{O}_0(G)$ and the proper type graph $\mathcal{T}_0(G)$. We show that all those graphs are quotient of $\mathcal{P}_0(G)$ and demonstrate a strong link between them dealing with $G=S_n$. We find simultaneously $c(\mathcal{P}_0(S_n))$ as well as the number of components of $\widetilde{\mathcal{P}}_0(S_n)$, $\mathcal{O}_0(S_n)$ and $\mathcal{T}_0(S_n)$

Evaluation of Computer-Based Management Information Systems Effectiveness

Shaker A. Zahra is a Graduate Instructor and Research Assistant and Ph. D. candidate in Management, Department of Management and Marketing, The University of Mississippi

Protein Recovery and Coagulation Properties of Commercial and Fractionated Milk Clotting Enzymes

Protein recovery and coagulation properties of five commercial and fractionated milk clotting enzymes were studied. The fractionated enzymes were Sephadex G-100 fractions of the commercial enzymes. Milk clotting activity of each fraction was tested using Berridge substrate. All fractions from each preparation which had milk clotting activity as measured with the Formagraph were collected and pooled. These samples and the original enzyme preparations were used to coagulate milk. Percent of protein lost in whey was determined by Kjeldahl. Coagulation was followed using a spectrophotometer monitoring changes in apparent absorbance at 600 nm. Curd protein yields using the five original enzyme preparations were compared with each other. Also, protein lost in whey from the five original preparations were compared with those using the isolated fraction. There was a significant difference among the original enzymes in protein lost in whey. There were also significant differences between some of the commercial enzyme preparations and their fractionated preparations. Gel filtration through Sephadex G-100 improved bovine rennet and calf rennet/porcine pepsin mixture more than the other three enzyme preparations. Calf rennet, Mucor miehei protease and modified M. miehei protease showed no significant reduction in protein lost to whey after fractionation. Protein loss using original calf rennet, bovine rennet and modified M. miehei protease were not significantly different from each other. M. miehei protease and calf rennet/porcine pepsin mixture were not significantly different from each other, but, the two groups were significantly different from each other. There were noticeable differences in coagulation curves of the five original enzymes. Coagulation properties of commercial and fractionated enzyme were different in all five pairs

Brexit can have profound implications for firms on both sides of the Atlantic

Since 2010, 9% of foreign US affiliates' profit has come from the UK, write Douglas Cumming and Shaker A. Zahr

Therapeutics formulated to target cancer stem cells: Is it in our future?

With the political, social and financial drives for cancer research, many advances have been made in the treatment of many different cancer types. For example, given the increase in awareness, early detection, and treatment of breast and prostate cancers, we have seen substantial increases in survival rates. Unfortunately there are some realms of cancer that have not seen these substantial advancements, largely due to their rapid progression and the inability to specifically target therapy