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The present study describes the effects of losartan and the angiotensin-converting enzyme inhibitor enalapril on blood pressure, echocardiographically calculated left ventricular mass, renal function evaluated by glomerular filtration rate and quality of life. The renin-angiotensin-aldosterone system is of importance for cardiovascular growth. There is substantial experimental documentation in animals that the angiotensin II antagonist, losartan, decreases the cardiac hypertrophy response caused by elevated arterial pressure as well as intravascular volume overload. However, data in humans is scarce. This is a 3-year, randomised, doubleblind study with parallel group design in 50 patients with essential hypertension. The results show that both drugs reduced blood pressure equally effectively, and also left ventricular mass (P Ͻ 0.001). After 3 years of treatment glomerular filtration rate significantly increased with losartan (P Ͻ 0.005). Serum uric acid fell modestly although significantly, dose-dependent in los-

A B S TRACT: Proteins (catalase, albumin, pepsin and lysozyme with different molecular weights and isoelectric points) were differently adsorbed at pH 7.0 on the clay fraction of three raw Nasaturated smectites (Crook and Uri montmorillonites and one hectorite). The adsorption isotherms of proteins on clay minerals showed typical Langmuir characteristics. Lysozyme was adsorbed under the effect of electrostatic interactions between the opposite charges of clay surfaces and protein molecules, whereas catalase and albumin were adsorbed under the effect of non-electrostatic forces. Pepsin was held in relatively high amounts only on the surfaces of hectorite. Proteins were intercalated in the interlayers spaces of smectites, usually undergoing extensive unfolding. Proteinsmectite complexes showed different behaviour to heating treatment. Some complexes remained practically unchanged after heating at 200~ Presence of 'wrecks' of interlayered materials was found after heating at 500~ for two hours. The amounts of proteins adsorbed on the external and interlamellar surfaces of clay minerals, partially coated with OH-A1 species, were much lower than those fixed on the clean clays. Only lysozyme was intercalated in chlorite-like complexes.In the last 40 years, adsorption of proteins on clay minerals has received the attention of many researches with diverse interests. The capacity of proteins to be sorbed is influenced by pH of the system, surface area of the clay minerals (kaolinite, illite, montmorillonite), isoelectric point (iep) of proteins, cation exchange capacity (CEC) of minerals, nature of cation saturating the clays, and temperature (McLaren et aL,