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The paper compares the existence of a crisis of medicine (characterised by a lack of assessment mechanisms of the medical treatment outcomes and their health alternatives) with a health crisis (characterised by the existence of health's determinants outside the health service area and the increase in the health demand) and the need to search for adequate solutions in order to solve them. We approach the problem from different standpoints. First, we search for ideas in the free market. Second, we propose several considerations on the "Health Maintenance Organisation" (HMOs) in the USA as well as on their limitations. Third, we study the radical proposals of change in Spain, Holland and the United Kingdom with the problems that competition can bring about, emphasizing the current difficulties in the British reforms and the lessons to consider from the Spanish case. Finally, the author concludes by pointing out the need for a more efficient use of resources and a better choice of priorities in Health.

A design equation is presented for packed-bed reactors containing immobilized enzymes in spherical porous particles with internal diffusion effects and obeying reversible one-intermediate Michaelis-Menten kinetics. The equation is also able to explain irreversible and competitive product inhibition kinetics. It allows the axial substrate profiles to be calculated and the dependence of the effectiveness factor along the reactor length to be continuously evaluated. The design equation was applied to explain the behavior of naringinase immobilized in Glycophase-coated porous glass operating in a packed-bed reactor and hydrolyzing both p-nitrophenyl-alpha-L-rhamnoside and naringin. The theoretically predicted results were found to fit well with experimentally measured values.

The use of the p-nitrophenyl-alpha-L-rhamnopyranoside for the specific measurement of the alpha-rhamnosidase activity of naringinase, by colorimetrically following the appearance of p-nitrophenolate anion, is proposed. Use of this synthetic substrate did not change the pH, temperature, or ionic strength optima of the enzyme. It did, however, result in (a) a decrease of the Michaelis constant of the enzyme, allowing the Vmax to be measured, this being impossible to accomplish with naringin, (b) an increase in the sensitivity of the assay to the presence of inhibitors in the reaction media, (c) an increase in the sensitivity which enabled measurement of low levels of naringinase due to the high absorptivity of p-nitrophenolate, and (d) a quick and cheap method of evaluating the alpha-rhamnosidase activity of naringinase.