Environmental Constraints, Commodity Mix, And Research Resource Allocation
The purpose of this paper is to show how the allocation of research resources among commodities and the effects of such allocations on the output mix depend upon (a) the initial production conditions, (b) the nature of the research production functions, (c) the nature of the demand relations for the commodity outputs, (d) relative factor endowments, and (e) the existence of different types of environmental constraints. The basic model used is a two-factor, two-product model in which certain types of technical change are introduced.
Market Integration: A Study of Sorghum Prices in Western India
This article examines the popular view in underdeveloped countries that there exist large regional price differences that are caused by speculative elements in trade. The data bearing on the prices of sorghum in a number of primary and terminal markets in India suggest that these differences are not caused by the activities of the traders. The analysis emphasizes the high degree of interdependence between wholesale markets in the process of price formation. Regional price differences often result from differences in varieties of the grain traded. Prices for the same product may differ because of transport costs. Price discrepancies of the order larger than transport costs may result from such factors as transport bottlenecks and government control on the movement of goods.
Adsorption of immunoglobulin Y in supermacroporous continuous cryogel with immobilized Cu(2+) ions.
The influence of temperature, pH and ionic strength on the adsorption of Immunoglobulin Y (IgY) in IDA-Cu(2+) cryogel system was studied by batch equilibrium measurements. The adsorptive equilibrium data were obtained at 17 and 27°C, pH 5.0 and 6.5, and at ionic strength of 50 and 200mmolL(-1) NaCl. Langmuir, Freundlich and Langmuir-Freundlich models were fitted to equilibrium data, while the enthalpy of adsorption of IgY in IDA-Cu(2+) cryogel system was calculated through Van't Hoff analysis. The binding of IgY on cryogel was stronger at 27°C and lowest pH and ionic strength values, with apparent maximum adsorption capacity of 27mgg(-1). The adsorption of protein in the resin was spontaneous in all analyzed cases. The results provide valuable information to enable the improvement of IgY purification processes.