Abstract
The use of immobilised metal-ion affinity chromatography with Cu 2+-iminodiacetate-Sepharose 6B as an affinity sorbent for the separation of endopeptidases and exopeptidases from the culture filtrates of Aspergillus niger is discussed. The performance of the affinity sorbent in relation to reproducibility of results and the effect of ballast substances on protein uptake were studied. The nature of the adsorption isotherms obtained with carboxypeptidase I and the semi-purified extract, containing acid protease, carboxypeptidases, pigments and various other contaminating substances, are compared. The partition coefficient, K d, of the affinity system with respect to carboxypeptidase I was determined and the dissociation constant, K L, of the carboxypeptidase I-Cu 2+-iminodiacetate complex was deduced.
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.
