[Effect of the medium on functional and structural properties of serum albumins. IV. The state of human serum albumin in the pH range from 5 to 10].

In order to investigate the effects of temperature and ionic strength on the N-B-transition and the alkaline denaturation of the human serum albumin, the pH-dependences of fluorescence position and relative yield of Trp-24 and of protein bound dye ANS were measured. The measurements were carried out at temperatures from 10 to 45 degrees C and ionic strengths (NaCl) from 0.001 to 0.

[The effect of the medium on the functional and structural properties of serum albumins. III. Relation between the N-F1-, F1-F2- and F2-E transitions of human serum albumin and temperature and ionic strength].

Using fluorescence parameters of tryptophanyl and bound ANS, the acid-induced structural transitions of defatted monomeric human serum albumin were measured as pH-dependences from 6 to 2.5 in the wide range of temperature (10 to 45 degrees C) and ionic strength (from 0.001 to 0.

[The effect of medium on functional and structural properties of serum albumins. II. The effect of temperature on the N-form of human serum albumin].

In order to investigate effects of temperature in the physiological range (from 10 to 50 degrees C) on structural, physical and functional properties of the N-form of human serum albumin (HSA), the temperature dependences of fluorescence parameters of Trp-214 residue of HSA and of the specifically bound dye ANS, as well as of association constants of ANS binding in the primary and secondary binding sites on HSA molecule were measured. The temperature-induced changes of these properties of HSA are essentially dependent on pH (7.0 or 5,6) and ionic strength (0.

[Effect of the medium on the functional and structural properties of serum albumins. I. Effect of ionic strength on N-variant of human serum albumin].

The effect of ionic strength on the 1-anilino-8- naphtalene sulfonate (ANS) binding sites of the N-form of human serum albumin (HSA) was studied by means of the protein and ligand fluorescence. The parameters of the binding of ANS to HSA (the number of sites and the binding constants) were determined by two methods: by measuring the ANS fluorescence either (i) at increasing protein concentrations and constant ANS concentration, or (ii) at increasing ANS concentration and two constant protein concentrations (9.6 and 2.