Abstract
Renin granules were isolated from rat kidney cortex by a continuous polyvinyl-pyrrolidone-coated colloidal silica (Percoll) density gradient centrifugation. A major peak of renin activity was found at a density of 1.12-1.13 g/ml, and the specific activity of renin in the peak fraction was increased by approximately 70-fold, as compared with that in the kidney cortex homogenate. On the other hand, activities of other reference enzymes, such as succinate dehydrogenase, acid phosphatase and glucose-6-phosphatase, were not detectable in the peak fraction. When the extract of the peak fraction was applied to a pepstatin column, trypsin-activated renin could not be detected in the breakthrough fractions. These results indicate that renin granules of the rat kidney cortex contain only active renin.
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.
