[Dependence of pepsin conformational states on pH and temperature].
A conformational behaviour of pepsin depending on pH and temperature was studied by circular dichroism, differential UV-spectroscopy, calorimetry and enzymatic hydrolysis kinetics. A subtile conformational transition of the enzyme accompanied by changes in the physico-chemical and enzymatic properties of the protein was observed within the temperature interval of 15--40 degrees and within the pH range of 1,1--5,6. The range of pepsin heat denaturation was studied. A diagram of pepsin conformational states under different values of pH and temperature was built.
D002151:Calorimetry; D002942:Circular Dichroism; D006863:Hydrogen-Ion Concentration; D007700:Kinetics; D010434:Pepsin A / Q000378:metabolism; D011487:Protein Conformation; D013056:Spectrophotometry, Ultraviolet; D013696:Temperature
D010434:Pepsin A
Konformatsionnye sostoianiia pepsina v zavisimosti ot pH i temperatury.