Abstract
Pholiota nameko polysaccharide (PNPS-1) has been isolated and purified by enzyme hydrolysis, hot water extraction, ethanol precipitation, ion-exchange chromatography and gel-filtration column chromatography. The inhibition of bovine pancreas ribonuclease (RNase A) by PNPS-1 has been studied to elucidate the mechanism responsible for the decreased activity. PNPS-1 was effective in a linear mixed-type inhibition as suggested from the Lineweaver–Burk plot, Dixon plot and their replots. The values of K i and αK i were estimated as 299.92 and 545.71 μM, respectively. The αK i was greater than K i indicating that noncompetitive inhibition was predominant over competitive inhibition.
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 callMore From: International Journal of Biological Macromolecules
Disclaimer: 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.
