Abstract
D-Alanine carboxypeptidase hydrolyzes the terminal D-alanyl-D-alanine peptide bond present in the pentapeptide: UDP-MurNac-L-Ala-D-Glumeso-Dap-D-Ala-o-Ala that is utilized for the biosynthesis of bacterial cell wall peptidoglycan. Because the enzyme from various species is inhibited either reversibly or irreversibly by extremely low concentration of penicillin, many studies on the mechanism and mode of action of penicillin have been directed toward this enzyme. Some of the conjugates adsorb the enzyme irreversibly and enzymatic activity could not be eluted by high salt concentrations. Exhaustive saturation of the gel by considerable amounts of the crude carboxypeptidase converted the penicillin-Sepharose column to a reversible adsorbant of the enzyme, suitable for affinity chromatography as described in the chapter. The “saturation” effect was highly specific, because no other protein, e.g., bovine serum albumin, could replace D-CPase in the the treatment.
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.
