The Amino Acid Sequence of Hypertensin Ii

Abstract

The pressor substance hypertensin, which has been found in the blood of many human beings with hypertensive cardiovascular disease (1), as well as in animals with experimental renal hypertension (2), may actually exist in two forms (3). The first form, hypertensin I, is the initial product of the action of the renal enzyme renin upon its plasma substrate and is not a vasoconstrictor or a directly pressor substance. It may be rapidly changed to the second form, hypertensin II, by a chloride-activated converting enzyme contained in the plasma. Hypertensin II is an extremely powerful vasoconstrictor material and is therefore the effector substance of the renin-hypertensin system (4, 5).Hypertensin I has been isolated from horse blood in a highly purified form (6). This material was treated with partially purified converting enzyme (4, 7) and after countercurrent distribution of the products, homogenous hypertensin II as well as a biologically inactive peptide residue was obtained. Quantitative amino acid analysis (8, 9) of these three substances together with the use of the enzyme carboxypeptidase (9) allowed the conversion to be expressed as a balanced biochemical equation.Hypertensin I converting enzyme hypertensin II + dipeptide

A Modern Understanding of the Traditional and Nontraditional Biological Functions of Angiotensin-Converting Enzyme

“…ACE was found to release the carboxyl-terminal histidyl-leucine of angiotensin I in producing angiotensin II (Lentz et al, 1956). This burst of biochemical investigation led to the amino acid sequence of angiotensin II, its laboratory synthesis, and ultimately the wide availability of this peptide, which facilitated enormous progress in understanding the pharmacology and physiology of the RAS (Elliott and Peart, 1956;Skeggs et al, 1956c;Bumpus et al, 1957;Rittel et al, 1957).…”

International Union of Basic and Clinical Pharmacology. XCIX. Angiotensin Receptors: Interpreters of Pathophysiological Angiotensinergic Stimuli

“…An identical vasoactive compound identified in Goldblatt hypertensive dog ischemic kidney by Braun-Menendez was named "hypertensin." The independently isolated pressor substance was later shown to be an octapeptide and not its decapeptide precursor (Skeggs et al, 1956;Bumpus et al, 1957;Elliott and Peart, 1957). Now the octapeptide bears the hybrid name angiotensin II (AngII) in honor of the original independent discovery of this important endocrine hormone with numerous actions beyond its hypertensive effects.…”

The renin-angiotensin system in the year 2000

“…The amino acid sequences of bovine and equine angiotensin were elucidated respectively by Elliott and Peart, 14 and by Skeggs et al 15 Angiotensin was shortly afterwards synthesised by Schwyzer and colleagues.…”