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SCP0019

Sigma-Aldrich

[Val5,Asn9]-Angiotensin I bullfrog

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About This Item

Empirical Formula (Hill Notation):
C59H86N16O15
Molecular Weight:
1259.41
UNSPSC Code:
12352209
NACRES:
NA.77

Assay

≥95% (HPLC)

form

lyophilized

composition

Peptide Content, ≥65%

storage condition

protect from light

storage temp.

−20°C

Amino Acid Sequence

Asp-Arg-Val-Tyr-Val-His-Pro-Phe-Asn-Leu

Application

Angiotensins are peptide hormone components of the renin-angiotensin system involved in the regulation of blood vessel constriction and aldosterone release. Angiotensin I, a decapeptide derived from angiotensinogen, is a converted to Angiotensin II by the removal of the two C-terminal amino acids. Various analogues of Angiotensin I may be used as substrates to identify, differentiate and characterize angiotensin-converting enzyme(s) (ACE).

Storage Class Code

11 - Combustible Solids

WGK

WGK 1

Flash Point(F)

Not applicable

Flash Point(C)

Not applicable

Certificates of Analysis (COA)

Search for Certificates of Analysis (COA) by entering the products Lot/Batch Number. Lot and Batch Numbers can be found on a product’s label following the words ‘Lot’ or ‘Batch’.

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M Bramucci et al.
The American journal of physiology, 273(6 Pt 2), R2089-R2096 (1998-01-22)
Our aim was to study the role of angiotensin-converting enzyme (ACE) and angiotensin II (ANG II) on ovarian steroidogenesis and prostaglandin production of amphibian. Hormonal effects of ACE, ACE inhibitors, synthetic bullfrog angiotensin I (ANG I), and [Val5]ANG II were
T Yamaguchi et al.
Journal of pharmacobio-dynamics, 9(7), 585-592 (1986-07-01)
In the present investigation, the occurrence of angiotensin I converting enzyme (EC 3.4.15.1; ACE) was first demonstrated in the kidney of bullfrog (Rana catesbeiana). Namely, a large amount of hydrolyzing activity toward N alpha-hippuryl-L-His-L-Leu-OH (HHL), a synthetic substrate of ACE
A Miano et al.
Acta physiologica Scandinavica, 160(3), 277-282 (1997-07-01)
The occurrence of angiotensin converting enzyme (EC 3.4.15.1; ACE) was demonstrated for the first time in serum of newt (Triturus carnifex) and frog (Rana esculenta). The enzymatic activity was evidenced following hydrolysis of N-[3-(2-furyl) acryloyl]L-phenylalanyl glycyl glycine (FAPGG), a synthetic

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