Literature DB >> 397194

Separation of dog brain renin-like activity from acid protease activity.

M Y Osman, R R Smeby, S Sen.   

Abstract

A renin-like enzyme and acid protease (cathepsin) from whole and saline-pefused dog brains were separated by CM-cellulose chromatography with a linear NaCl gradient. Plasma renin and cathepsin were also separated using the same system. During the separation steps (in all the above cases) the specific activity of the brain renin-like enzyme was increased, while the specific activity of the brain cathepsin was decreased. Approximately a 70-fold increase in the specific activity of brain renin-like enzyme and a sixfold decrease in brain cathepsin specific activity was obtained from saline-perfused brain. The separation made it possible to study the pH optimum of the brain renin-like enzyme and acid protease. The brain renin-like enzyme showed optimal activity in the range of pH 6-7. Immunologically, the renin-like enzyme was distinctly different from dog kidney renin.

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Year:  1979        PMID: 397194     DOI: 10.1161/01.hyp.1.1.53

Source DB:  PubMed          Journal:  Hypertension        ISSN: 0194-911X            Impact factor:   10.190


  2 in total

1.  Expression of the renin gene in extra-renal tissues of the rat.

Authors:  N J Samani; J D Swales; W J Brammar
Journal:  Biochem J       Date:  1988-08-01       Impact factor: 3.857

2.  Distribution of renin activity and angiotensinogen in rat brain. Effects of dietary sodium chloride intake on brain renin.

Authors:  C P Genain; G R Van Loon; T A Kotchen
Journal:  J Clin Invest       Date:  1985-11       Impact factor: 14.808

  2 in total

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