Abstract
Phosphatase activity, using p-nitrophenyl phosphate (NPP) as the substrate, was inhibited by myo-inositol hexaphosphate (phytate). The extent of inhibition by 5mm phytate of the alkaline phosphatase activity of calf intestine and Escherichia coli, and of the acid phosphatase activity of wheat germ was 82, 56 and 50%, respectively. However, acid phosphatases from rice bran were not inhibited by 10mm phytate. The effect of preincubation with phytate on the acid and alkaline phosphatase activity was investigated. After a 180-min preincubation with 1 mm phytate, the extent of inhibition was 98% for the calf intestine enzyme, 88% for the E. coli enzyme, and 75% for the wheat germ enzyme. Mg2+ enhanced the phosphatase activity, but the addition of phytate lowered it. The inhibition of E. coli alkaline phosphatase by phytate was noncompetitive, with an apparent inhibitor constant of 0.45 mm under the assay conditions. The inhibition of calf intestine alkaline phosphatase and of wheat germ acid phosphatase was of...
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.
