Data set on effect of amaranth proteins on the RAS system. , and assays.

Data set presented in this article is related to the research paper entitled "Effect of amaranth proteins on the RAS system. and assays", available in Food Chemistry [1]. In this article, we evaluated the effect on systolic blood pressure of spontaneously hypertensive rats (SHR) of different samples with amaranth proteins/peptides.

Effect of amaranth proteins on the RAS system. In vitro, in vivo and ex vivo assays.

The aim of this work was to analyse the hypotensive effect of amaranth protein/peptides on spontaneously hypertensive rats (SHR). The mechanism of action of these peptides was studied in vivo and ex vivo. We also tested the effect of protection against gastrointestinal digestion (GID) exerted by an O:W emulsion on the integrity of the antihypertensive peptides.

Broken Rice as a Potential Functional Ingredient with Inhibitory Activity of Renin and Angiotensin-Converting Enzyme(ACE).

The aim of this work was to evaluate the ability of broken rice, an underutilized industrial by-product, as a potential functional and health promoting ingredient. With this purpose, the ability to inhibit the angiotensin converting enzyme and renin of a rice protein hydrolyzate (RPH) obtained from a high-protein variety of broken rice (var. Nutriar FCAyF) was analyzed (IC = 0.

In Vitro Modulation of Renin-Angiotensin System Enzymes by Amaranth (Amaranthus hypochondriacus) Protein-Derived Peptides: Alternative Mechanisms Different from ACE Inhibition.

Among the factors affecting the development of cardiovascular diseases, hypertension is one of the most important. Research done on amaranth proteins has demonstrated their hypotensive capacity in vivo and in vitro; nevertheless, the mechanism underlying this effect remains unclear. The aim of this study was to analyze in vitro the inhibition of peptides derived from an amaranth hydrolysate (AHH) on other RAS enzymes other than ACE.

Physicochemical, functional and angiotensin converting enzyme inhibitory properties of amaranth (Amaranthus hypochondriacus) 7S globulin.

Background: Amaranth 7S globulin is a minor globulin component and its impact on the properties of an amaranth protein ingredient depends on its proportion in the variety of amaranth being considered. Some physicochemical, functional and angiotesin I-converting enzyme (ACE) inhibitory properties of amaranth vicilin were studied in this work and compared with the 11S globulin.

Results: Fluorescence spectroscopy results indicated that 7S globulin tryptophans were more exposed to the solvent and, by calorimetry, the 7S globulin denaturation temperature (T(d) ) was found lower than the 11S globulin T(d) , suggesting a more flexible structure.

Structural modifications of Amaranth proteins during germination.

Amaranth storage proteins begin to be hydrolyzed immediately following the completion of germination. Albumins and globulins (7S globulin, 11S-globulin and globulin-p) were formerly modified, and glutelins, the most aggregated fraction, later. Globulins mobilization starts with the proteolysis of the 7S like-globulin polypeptides and the propolypeptide and acid (A) polypeptides of 11S-globulin and globulin-p.

Role of peroxidase inhibition by insulin in the bovine thyroid cell proliferation mechanism.

Monolayer primary cultures of thyroid cells produce, in the presence of insulin, a cytosolic inhibitor of thyroid peroxidase (TPO), lacto peroxidase (LPO), horseradish peroxidase (HRPO) and glutathione peroxidase (GPX). The inhibitor, localized in the cytosol, is thermostable and hydrophylic. Its molecular mass is less than 2 kDa.

Surface physicochemical properties of globulin-P amaranth protein.

Globulin-P, the polymerized 11S amaranth globulin, is composed of 280 kDa unitary molecules (UM, 23%) and aggregates larger than 500 kDa (A, 70%). Antibodies against these proteins were prepared to study their surface characteristics and to assess their homology with other storage proteins. Results showed that globulin-P unitary molecules and aggregates had similar reactive surfaces.