Abstract
1. 1. The small-size adenosine deaminases ( M r = 35,000 and 43,000 ) in calf intestinal mucosa, frog liver and scallop adductor muscle and the large-size deaminase ( M r = 100,000 ) in frog liver probably formed by adding a conversion protein to the small enzyme, were tightly bound to the purine riboside affinity column. 2. 2. Binding of the other large-size enzymes ( M r = 140,000 ) in the midgut gland of scallop and mussel to the column was not successful. 3. 3. It seems that the binding difference does not depend on a change in affinity between active site and ligand but rather on the stereospecific positioning of active site in the enzyme molecules.
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: Comparative Biochemistry and Physiology -- Part B: Biochemistry and Molecular Biology
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.
