PMID: 38848Aug 15, 1979

Physicochemical properties of non-activated and activated renin from human amniotic fluid

Biochimica Et Biophysica Acta
T ItoP Corvol

Abstract

The main physicochemical and enzymic properties of non-activated and activated human amniotic renin (EC 3.4.99.19) were studied in order to clarify the relationships between the two enzymes. Human amniotic renin was activated by dialysis against acidic buffer (pH 3.3), direct acidification or trypsin treatment. All procedures produced similar activation. The physicochemical characteristics of non-activated and activated renin were compared to those of human renal renin. Non-activated renin had a molecular weight of 45,500. A similar molecular weight was obtained by gel eluate activation and by acid treatment of renin prior to gel filtration. Similar isoelectric points were also found for non-activated and activated renin. One major renin peak focused at pH 6.6, whereas no similar renin peak was detected in extracts from normal human kidney. In addition, non-activated and activated renin forms were found to have the same optimal pH, the same Km and the same inhibiting pepstatin concentrations.

References

Jun 1, 1975·The Journal of Clinical Endocrinology and Metabolism·R P DayC M Gonzales
Jun 1, 1975·The Journal of Clinical Endocrinology and Metabolism·R P Day, J A Luetscher
Jul 1, 1978·The Journal of Clinical Endocrinology and Metabolism·E E Slater, E Haber
Jun 1, 1979·The Journal of Clinical Endocrinology and Metabolism·F X GalenJ Menard
May 1, 1974·The Journal of Clinical Endocrinology and Metabolism·R P Day, J A Luetscher
Feb 7, 2012·European Journal of Radiology·Tetsuya FujigaiTakamichi Murakami

Related Concepts

Amniotic Fluid Index
SDS-PAGE
Enzyme Activation
Hydrogen-Ion Concentration
Preprorenin

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