Year-end Sale % OFF 
Abstract
In the present study we report on a rapid two-step affinity chromatographic procedure to purify aldose reductase from human and rat kidney papilla and inner medulla. This enzyme, which is responsible for sorbitol formation in the kidney, was purified 145-fold from rat and 76-fold from human kidneys by consecutive Blue Sepharose and Matrex Orange chromatography. SDS-PAGE showed a single band of 38 kD for the human enzyme and a doublet of similar molecular weight for the rat kidney aldose reductase. The enzyme was characterized by substrate specificity and kinetic constants found identical to that of other organs purified previously.
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.
