Abstract
1. 1.|The sucrase isomaltase complex has been isolated from rabbit small intestine. The procedure involves urea extraction of the whole intact small intestine, papain solubilization, and chromatography on Sephadex G-200 and polyacrylamide-gel (Bio-Gel P-300). 2. 2.|The chromatography on Sephadex G-200 is apparently based on an interaction of the substrate-enzyme type. 3. 3.|Sucrase-isomaltase, as isolated here, carries at least two substrate sites: one splitting sucrose and maltose, the other splitting isomaltose, palatinose and probably maltose also. 4. 4.|Na + is a non-essential activator. It increases the maximum velocity by some 20–30%, with minor or no change of the apparent K m for sucrose. 5. 5.|Tris is a strong fully competitive inhibitor. 6. 6.|The inhibition by some metals, and the lack of inhibition by other metals or by p-chloromercuribenzoate, indicate that SH groups are not required for full enzyme activity, whereas an imidazole group may be required.
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.
