[pH-dependence of fluorescence parameters of chymotrypsin, chymotrypsinogen, trypsin and lysozyme].
The alterations of tryptophan fluorescence parametres with pH may be due to: 1) conformational changes; 2) changes in the ionic state of groups capable of quenching the tryptophan fluorescence. The applications of the model of discrete forms of tryptophan allow one to separate these mechanisms and estimate the middle points of conformational changes and pK's of quenching groups. For chymotrypsin (CT) and chymotrypsinogen (CTG) conformational changes were registrated with middle points: CT pH 4.1 and 8.8; CTG -- pH 3.2 and 9.8, and pK's of histidines: CT -- 5.4 and 6.6; CTG -- 5.6 and 7.0. For trypsin conformational changes were shown with middle points: pH 3.2; 5.8; 8.5 and for lysozyme -- pH 5.9.
D002918:Chymotrypsin; D002919:Chymotrypsinogen; D006863:Hydrogen-Ion Concentration; D009113:Muramidase; D011487:Protein Conformation; D013050:Spectrometry, Fluorescence; D014357:Trypsin
D002919:Chymotrypsinogen; D009113:Muramidase; D002918:Chymotrypsin; D014357:Trypsin
Zavisimost' Parametorov fluorestsentsii khimotripsina, khimotripsinogena, tripsina i lizotsima ot velichiny pH.