Abstract
Evidence was sought to characterize further the nature of the uncompetitive stereospecific inhibition of rat intestinal alkaline phosphatase by l-phenylalanine. That it is nonallosteric is clear from (1) the hyperbolic curves relating inhibition as a function of inhibitor or substrate concentration; (2) the persistence of inhibition after the tertiary structure of the enzyme protein molecule had been altered by heat denaturation, papain digestion and treatment with urea or stilbestrol; (3) the relatively low entropy change of −6.7 entropy units per mole; (4) the figure of unity for n, the number of l-phenylalanine molecules which combine with one molecule of enzyme. However, this inhibition may represent an example of McElroy's homosteric transition since the extent of l-phenylalanine inhibition decreases with an increase in temperature and the optimal temperature for maximal velocity is raised in digests containing l-phenylalanine.
Sign-in/Register to access full text options 
Talk to us
Join us for a 30 min session where you can share your feedback and ask us any queries you have
Schedule a callDisclaimer: All third-party content on this website/platform is and will remain the property of their respective owners and is provided on "as is" basis without any warranties, express or implied. Use of third-party content does not indicate any affiliation, sponsorship with or endorsement by them. Any references to third-party content is to identify the corresponding services and shall be considered fair use under The CopyrightLaw.
