THE PREPARATION AND FUNCTION OF THE HYPERTENSIN-CONVERTING ENZYME
@article{Skeggs1956THEPA, title={THE PREPARATION AND FUNCTION OF THE HYPERTENSIN-CONVERTING ENZYME}, author={Leonard T. Skeggs and Joseph R. Kahn and Norman P. Shumway}, journal={The Journal of Experimental Medicine}, year={1956}, volume={103}, pages={295 - 299} }
It has been shown by use of isolated, perfused rat kidneys that hypertensin II is a potent vasoconstrictor substance while hypertensin I is not. Hence it would appear that in intact animals the pressor activity of hypertensin I results from its rapid conversion to hypertensin II. An enzyme which effects this conversion has been procured from horse plasma in a semipurified form by means of ammonium sulfate fractionation and isoelectric precipitation. A method is described for estimating the…
956 Citations
RENAL pressor system in hypertension.
- Biology, MedicineMedical bulletin
- 1957
Two different chemical forms of the material have been obtained in purified form and their chemical constitution deter- mined, and the initial product of the action of renin on its substrate is the decapetide hypertensin I.
THE AMINO ACID COMPOSITION OF HYPERTENSIN II AND ITS BIOCHEMICAL RELATIONSHIP TO HYPERTENSIN I BY KENNETH E. LENTZ, PH.D.,
- Biology, Chemistry
- 2003
Hypertensin II, formed by the action of the converting enzyme on hypertensin I, was shown to be the substance responsible for vasoconstriction and the elevation of blood pressure produced by the renin-hypertens in system.
THE PURIFICATION OF HYPERTENSIN II
- BiologyThe Journal of experimental medicine
- 1956
Improved methods are presented for the preparation of renin and its substrate, as well as in methods for the reaction of these materials and the purification of the resulting hypertensin I.
Conversion of Angiotensin I to Angiotensin II by Cell-free Extracts of Dog Lung
- BiologyNature
- 1968
This communication describes some of the enzymes in extracts of dog lung that metabolize angiotensins I and II and particularly those catalysing the conversion ofAngiotensin I to angiotENSin II (“converting enzyme”) and the enzyme(s) responsible for the inactivation of ang Elliotensin II and angiotsin I are referred to as “destroying enzyme’.
In vitro Production of Angiotensin I by Renal Glomeruli
- Biology, MedicineNature
- 1969
This communication summarizes the results and the unexpected finding that glomeruli produce a pressor substance distinct from renin.
Physiological Function and Catalytic Mechanism of Angiotensin Converting Enzyme
- Biology
- 1981
The clinical importance of ACE has been established by the discovery that synthetic inhibitors of this enzyme are potent drugs for the control of hypertension in man and the design of these inhibitors has been guided by a hypothetical model of the active site of ACE.
Purification of angiotensin I converting enzyme from pig lung using concanavalin-A sepharose chromatography.
- BiologyJournal of chromatography. B, Analytical technologies in the biomedical and life sciences
- 2003
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Two types of hypertensin have been demonstrated by means of counter-current distribution and a highly purified preparation containing horse hypertensins I and II caused an elevation of blood pressure when injected into human beings.
THE PURIFICATION OF HYPERTENSIN I
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- 1954
Acid hydrolysis and paper chromatography indicate in a preliminary fashion that there are about nine amino acids present in the intact polypeptide.
AMINO ACID COMPOSITION AND ELECTROPHORETIC PROPERTIES OF HYPERTENSIN I
- BiologyThe Journal of experimental medicine
- 1955
A preparation of hypertensin I was purified by countercurrent distribution and was shown to migrate as a single component in starch blocks at pH 9.3 and 4.2, and showed eight amino acids in approximately unimolar proportion.
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