Purification and characterisation of two forms of renin from human renal cortex

McIntyre, Gordon Douglas (1983) Purification and characterisation of two forms of renin from human renal cortex. PhD thesis, University of Glasgow.

Abstract

A new affinity column for renin was prepared by coupling the isosteric peptide inhibitor of renin, H.77 (D-His-Pro-Phe-His-LeuR-Leu-Val-Tyr, where R is a reduced peptide bond, -CH2-NH-), to activated 6-aminohexanoic acid-Sepharose 4B. Chromatography of a crude extract of human kidney cortex on this material resulted in a 5,500-fold purification of renin in 76% yield. The purified enzyme (specific activity 871 units/mg) was free of non-specific acid proteinase activity and was stable at pH 6.8 and -20

• Item Type: Thesis (PhD)
• Qualification Level: Doctoral
• Additional Information: Adviser: B J Leckie
• Keywords: Biochemistry
• Date of Award: 1983
• Depositing User: Enlighten Team
• Unique ID: glathesis:1983-72919
• Copyright: Copyright of this thesis is held by the author.
• Date Deposited: 11 Jun 2019 11:06
• Last Modified: 11 Jun 2019 11:06
• URI: https://theses.gla.ac.uk/id/eprint/72919