Actions for CARBON-13 KINETIC ISOTOPE EFFECTS IN THE UREASE-CATALYZED HYDROLYSIS OF UREA. I. TEMPERATURE DEPENDENCE

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CARBON-13 KINETIC ISOTOPE EFFECTS IN THE UREASE-CATALYZED HYDROLYSIS OF UREA. I. TEMPERATURE DEPENDENCE

Author
Lynn, K. R.
Published
[Place of publication not identified] : [publisher not identified], 1960.
[Oak Ridge, Tennessee] : [U.S. Atomic Energy Commission], 1960.
Physical Description
microopaque : positive ; 8 x 13 cm
Additional Creators
Yankwich, P. E.

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Summary
The C/sup 13/ kinetic isotope effects in the urease-catalyzed hydrolysis of urea were measured with several preparations of the enzyme in two buffers (maleic acid-maleate, and trishydroxymethyl amino methane-sulfuric acid) in which the kinetics were studied previously. The results indicate that the mechanism of the hydrolysis possesses complexities not reflected in the gross rate phenomena which do influence the isotope fractionation. The isotopic analogues of the several mechanisms found adequate to explain the kinetics of the reaction are examined in detail. It was concluded that complexity at the molecular level, probably involving temperature-dependent interconversion of two or more types of active sites (directly, or indirectly through enzyme conformational changes), is responsible for the isotope effect results obtained. (auth)
Report Numbers
TID-12800
Other Subject(s)
Collection
U.S. Atomic Energy Commission depository collection.
Note
NSA number: NSA-15-019230
OSTI Identifier 4005204
Research organization: Illinois. Univ., Urbana. Noyes Lab. of Chemistry.
View MARC record | catkey: 42249168