Benefits of irrigation water transfers in the National River Linking Project: a case study of Godavari (Polavaram)-Krishna link in Andhra Pradesh

River basin managementDevelopment projectsWater scarcityWater transferGroundwater irrigationSurface irrigationLand useDamsRiceLivestock

The virial expansion of a classical interacting system

We consider N particles interacting pair-wise by an inverse square potential in one dimension (Calogero-Sutherland-Moser model). When trapped harmonically, its classical canonical partition function for the repulsive regime is known in the literature. We start by presenting a concise re-derivation of this result. The equation of state is then calculated both for the trapped and the homogeneous gas. Finally, the classical limit of Wu's distribution function for fractional exclusion statistics is obtained and we re-derive the classical virial expansion of the homogeneous gas using this distribution function.Comment: 9 pages; added references to some earlier work on this problem; this has led to a significant shortening of the paper and a changed titl

Chiral symmetry breaking and stability of quark droplets

We discuss the stability of strangelets -- quark droplets with strangeness -- in the Nambu--Jona-Lasinio model supplemented by a boundary condition for quark confinement. Effects of dynamical chiral symmetry breaking are considered properly inside quark droplets of arbitrary baryon number. We obtain the energy per baryon number of quark droplets with baryon number from one to thousands. It is shown that strangelets are not the ground states as compared with nuclei, though they can be locally stable

Galactose-6-phosphate dehydrogenase. Purification and partial characterization

A new enzyme, galactose-6-phosphate dehydrogenase has been purified about 50-fold from goat liver. The enzyme can be distinguished from the nonspecific hexose-6-phosphate dehydrogenase and glucose-6-phosphate dehydrogenase by its high substrate specificity and absolute pyridine nucleotide requirement. In contrast to the hexose-6-phosphate dehydrogenase, this enzyme is located exclusively in the cytoplasmic fraction of the cell. The enzyme is a metalloprotein and is highly sensitive to mercurials. The product of the reaction is possibly a ketoaldose, phosphorylated at the primary alcoholic group

Presence of two conformationally vicinal sulfhydryl groups at the active site of UDP-glucose 4-epimerase from Saccharomyces fragilis

UDP-glucose 4-epimerase from Saccharomyces fragilis was inactivated by diazene dicarboxylic acid bis-N,N-dimethylamide or diamide, a compound that can specifically oxidize conformationally vicinal sulfhydryl groups on protein surfaces. The inactive enzyme was shown to retain the original dimeric structure and NAD, which is a coenzyme for this reaction, was not dissociated from the apoenzyme. The loss of activity was due to the direct modification of sulfhydryl groups and could not be attributed to any subsequent loss of structural integrity. The activity of the enzyme could be regained almost completely on incubation with mercaptoethanol alone and no exogenous NAD was needed for reactivation. The reactivated enzyme showed most of the characteristic properties of the native enzyme like activation by cations or inhibition by UMP. Presence of substrate provided partial protection against inactivation by the reagent. Formation of disulfide bond(s) across the subunits was demonstrated by sodium dodecyl sulfate gel electrophoresis in absence of mercaptoethanol. Titration of native and diamide-inactivated enzyme with p-chloromercuribenzoate revealed that only two sulfhydryl groups were involved in the formation of the disulfide cross-linkage across the subunits. The above results indicate the possible presence of two conformationally vicinal sulfhydryl groups at two different subunits of the enzyme that constitute part of the active site