[Comparative characteristics of hydrophobic nature of certain proteins by their interaction with 2-p-toluidinonaphthalene-6-sulfonates].
The hydrophobic nature of proteins is characterized by a degree of 2-p-toluidinonaphthalene-6-sulphonate (TNS) affinity to them and is pronounced quantitatively in the semi-saturated (C1/2) concentrations. This index correlates directly with the position of TNS emission maximum after the binding with proteins and reversely with the yield of fluorescence. The preparations of phosphofructokinase, lactate dehydrogenase, xantinoxidase, glyceratekinase, lysozyme, RNase during the long (1-2 h) contact with TNS change the values C1/2, that evidences for interaction with the hydrophobic indicator of new structures of protein molecule or for a change in the nature of its linkage itself. An attempt is made to characterize the accessible for TNS hydrophobic nature of individual proteins by a coefficient of molar hydrophobic nature which unites three mentioned characteristics. Serum albumin, insulin, glucogon, alpha chemotrypsin, DNase are most hydrophobic, pyruvate kinase, aldolase, urease, RNase--least hydrophobic, Glycerate kinase, pyruvate decarboxylase, phosphofructokinase, lactate dehydrogenase, alcohol dehydrogenase, xanthinoxidase, trypsin, lysozyme are in intermediate position.
D001665:Binding Sites; D009282:Naphthalenesulfonates; D011485:Protein Binding; D011487:Protein Conformation; D011506:Proteins; D014052:Toluidines; D014867:Water
D009282:Naphthalenesulfonates; D011506:Proteins; D014052:Toluidines; D014867:Water