The Elements of Input-Output Analysis

The first writers to treat economics systematically — Adam Smith and his immediate successors — dealt with the economy as a whole. In today’s terminology they were concerned with macroeconomics. Later economists, notably Alfred Marshall and his followers in the Neo-classical school, focused upon the household and the firm. They inaugurated the era of microeconomics which led to Chamberlin’s theory of monopolistic competition and Mrs. Robinson’s theory of imperfect competition. The Neo-classical economists and their successors analyzed the forces which result in economic equilibrium, but their approach was that of partial equilibrium, or the method of examining one thing at a time. During the 1930s, under the influence of John Maynard Keynes, there was a revival of interest in aggregative economics. Keynesians drew on the work of both Classical and Neo-classical schools. Like the latter, they were concerned with the forces which result in equilibrium or disequilibrium, but they returned to the Classical tradition in their emphasis on the economy as a whole. The Neo-classical economists had devoted much of their attention to the theory of value - examination of the forces which determine prices under given market conditions. The Keynesians, however, were primarily concerned with the determinants of income and employment. Their system was based on broad aggregates: total employment, total consumption, total investment, and national income. Keynesian economists showed how these variables are related to one another, and how changes in one affect the rest. They were much less interested than the Neoclassical economists in examining the effects of a change in one variable on the assumption that all others remained fixed. In this sense the Keynesians were concerned with general rather than partial equilibrium. But neither the Neo-classical economists nor the Keynesians were directly concerned with economic interdependence, with the structure of the economy and the way in which its individual sectors fit together.https://researchrepository.wvu.edu/rri-web-book/1005/thumbnail.jp

The impact of space and space-related activities on a local economy. a case study of boulder, colorado. part i- the input-output analysis

Impact of space and space-related activities on industry and general economy of Boulder, Colorad

Purification and characterization of recombinant pyruvate dehydrogenase kinases from pea and soybean plants [abstract]

Abstract only availableFaculty Mentor: Dr. Douglas Randall, BiochemistryThe pyruvate dehydrogenase complex (PDC) is a large multienzyme complex catalyzing the oxidative decarboxylation of pyruvate and concomitant reduction of NAD to yield acetyl-CoA and NADH. The plant PDCs have vital roles in catabolic and anabolic metabolism. The plant complexes contain three primary components: pyruvate dehydrogenase (E1), dihydrolipoyl acetyltransferase (E2) and dihydrolipoyl dehydrogenase (E3). Additionally, mitochondrial PDC (mtPDC) contains two associated regulatory enzymes: pyruvate dehydrogenase kinase (PDK) and phospho-pyruvate dehydrogenase phosphatase. PDK catalyzes phosphorylation on the subunit of E1, resulting in inactivation of the complex. We have cloned two PDKs from soybean and recently we have cloned three PDKs from pea. cDNAs encoding soybean PDK 1 and 2 and pea PDK 1, 2 and 3 were subcloned into pET expression vector and E. coli BL21 (DE3) cells were transformed with each pET-28-H6-PDK construct. Recombinant proteins were expressed and purified by Ni-NTA agarose column chromatography to approximately 95% homogeneity. Biochemical characterization of these proteins is underway.The pyruvate dehydrogenase complex (PDC) is a large multienzyme complex catalyzing the oxidative decarboxylation of pyruvate and concomitant reduction of NAD to yield acetyl-CoA and NADH. The plant PDCs have vital roles in catabolic and anabolic metabolism. The plant complexes contain three primary components: pyruvate dehydrogenase (E1), dihydrolipoyl acetyltransferase (E2) and dihydrolipoyl dehydrogenase (E3). Additionally, mitochondrial PDC (mtPDC) contains two associated regulatory enzymes: pyruvate dehydrogenase kinase (PDK) and phospho-pyruvate dehydrogenase phosphatase. PDK catalyzes phosphorylation on the a subunit of E1, resulting in inactivation of the complex. We have cloned two PDKs from soybean and recently we have cloned three PDKs from pea. cDNAs encoding soybean PDK 1 and 2 and pea PDK 1, 2 and 3 were subcloned into pET expression vector and E. coli BL21 (DE3) cells were transformed with each pET-28-H6-PDK construct. Recombinant proteins were expressed and purified by Ni-NTA agarose column chromatography to approximately 95% homogeneity. Biochemical characterization of these proteins is underway

Asp295 Stabilizes the Active-Site Loop Structure of Pyruvate Dehydrogenase, Facilitating Phosphorylation of Ser292 by Pyruvate Dehydrogenase-Kinase

We have developed an in vitro system for detailed analysis of reversible phosphorylation of the plant mitochondrial pyruvate dehydrogenase complex, comprising recombinant Arabidopsis thalianaα2β2-heterotetrameric pyruvate dehydrogenase (E1) plus A. thaliana E1-kinase (AtPDK). Upon addition of MgATP, Ser292, which is located within the active-site loop structure of E1α, is phosphorylated. In addition to Ser292, Asp295 and Gly297 are highly conserved in the E1α active-site loop sequences. Mutation of Asp295 to Ala, Asn, or Leu greatly reduced phosphorylation of Ser292, while mutation of Gly297 had relatively little effect. Quantitative two-hybrid analysis was used to show that mutation of Asp295 did not substantially affect binding of AtPDK to E1α. When using pyruvate as a variable substrate, the Asp295 mutant proteins had modest changes in kcat, Km, and kcat/Km values. Therefore, we propose that Asp295 plays an important role in stabilizing the active-site loop structure, facilitating transfer of the γ-phosphate from ATP to the Ser residue at regulatory site one of E1α