These tools will no longer be maintained as of December 31, 2024. Archived website can be found here. PubMed4Hh GitHub repository can be found here. Contact NLM Customer Service if you have questions.


PUBMED FOR HANDHELDS

Search MEDLINE/PubMed


  • Title: Relationship between state of a thermosensitive matrix and the activity of urease immobilized in it.
    Author: Kukhtin AV, Eremeev NL, Belyaeva EA, Kazanskaya NF.
    Journal: Biochemistry (Mosc); 1997 Apr; 62(4):371-6. PubMed ID: 9275275.
    Abstract:
    The effect of temperature on kinetic and equilibrium parameters of urea hydrolysis catalyzed with urease immobilized into a thermosensitive poly-N-isopropylacrylamide gel was studied. The temperature behavior of the gel-urease system is different from similar systems. After a decrease in the enzyme activity above the critical temperature, the maximal rate of the enzymatic reaction and gel swelling ratio begin to increase. Urea hydrolysis catalyzed with immobilized urease and shrinking-swelling of the thermosensitive urease-containing gel depend on each other. Under collapse, gel swelling increases due to the enzymatic reaction. The rate of the enzymatic reaction no longer follows Michaelis-Menten kinetics, and the dependence of the reaction rate on substrate concentration becomes more complicated.
    [Abstract] [Full Text] [Related] [New Search]