Nitric oxide is an inorganic free radical gas, of formula *N=O (abbreviated as NO). The discovery in 1987/88 that vascular endothelial cells are able to synthesize NO from L-arginine as a transcellular signal [1-4] was initially received by most biologists with considerable scepticism. By now, however, the existence of the L-arginine:NO pathway has been thoroughly documented and its relevance in biology is slowly being unravelled. All of this has led to the appearance of a new and vigorous field of research, as evidenced by the increasing number of publications relating to NO and NO synthases (Figure 1). This review will describe the known biochemical mechanisms involved in the synthesis of NO from L-arginine by the NO synthases and will also describe the nature of these enzymes, their inhibition and their molecular characteristics. For more extensive reviews about the biological roles of NO, see [5-7].

/pdf/nitric-oxide-synthases-in-mammals-1etyzijagx.pdf

Nitric oxide synthases in mammals.

Accumulation of an endogenous inhibitor of nitric oxide synthesis in chronic renal failure.

Background—Asymmetric dimethylarginine (ADMA) is an endogenous competitive inhibitor of nitric oxide (NO) synthase. Because endothelial NO elaboration is impaired in hypercholesterolemia, we investigated whether plasma concentrations of ADMA are elevated in young, clinically asymptomatic hypercholesterolemic adults. We further studied whether such elevation of ADMA levels was correlated with impaired endothelium-dependent, NO-mediated vasodilation and urinary nitrate excretion. In a randomized, double-blind, placebo-controlled study, we investigated whether these changes could be reversed with exogenous l-arginine. Methods and Results—We measured plasma levels of l-arginine, ADMA, and symmetrical dimethylarginine (SDMA) by high-performance liquid chromatography in 49 hypercholesterolemic (HC) and 31 normocholesterolemic (NC) humans. In 8 HC subjects, endothelium-dependent forearm vasodilation was assessed before and after an intravenous infusion of l-arginine or placebo and compared with 8 NC control subj...

Asymmetric Dimethylarginine (ADMA): A Novel Risk Factor for Endothelial Dysfunction Its Role in Hypercholesterolemia

http://www.positivedesigns.com/cardio/Arginine%20&%20Kidney%20Disease.pdf

Plasma concentration of asymmetrical dimethylarginine and mortality in patients with end-stage renal disease: A prospective study

An integral part of the safety assessment of genetically modified plants is consideration of possible human health effects, especially food allergy. Prospective testing for allergenicity of proteins obtained from sources with no prior history of causing allergy has been difficult because of the absence of valid methods and models. Food allergens may share physicochemical properties that distinguish them from nonallergens, properties that may be used as a tool to predict the inherent allergenicity of proteins newly introduced into the food supply by genetic engineering. One candidate property is stability to digestion. We have systematically evaluated the stability of food allergens that are active via the gastrointestinal tract in a simple model of gastric digestion, emphasizing the major allergens of plant-derived foods such as legumes (peanuts and soybean). Important food allergens were stable to digestion in the gastric model (simulated gastric fluid). For example, soybean beta-conglycinin was stable for 60 min. In contrast, nonallergenic food proteins, such as spinach ribulose bis-phosphate carboxylase/oxygenase, were digested in simulated gastric fluid within 15 sec. The data are consistent with the hypothesis that food allergens must exhibit sufficient gastric stability to reach the intestinal mucosa where absorption and sensitization (development of atopy) can occur. Thus, the stability to digestion is a significant and valid parameter that distinguishes food allergens from nonallergens.

Stability of food allergens to digestion in vitro

Occurrence of a new enzyme catalyzing the direct conversion of NG,NG-dimethyl-L-arginine to L-citrulline in rats.

Detection of NG, NG-Dimethylarginine Dimethylaminohydrolase in the Nitric Oxide-Generating Systems of Rats Using Monoclonal Antibody

Dimethylarginine:pyruvate aminotransferase in rats. Purification, properties, and identity with alanine:glyoxylate aminotransferase 2.

At least 15 allergenic proteins have been found in soybean using the sera of soybean-sensitive patients with atopic dermatitis [T. Ogawa et al., J. Nutr. Sci. Vitaminol., 35, 555-565 (1991)]. In the present study, a monoclonal antibody (mAb) against Gly m Bd 28K, one of the major allergens of soybean, was prepared, and Gly m Bd 28K was purified from defatted soybean flakes by five purification steps, including immunoaffinity chromatography with the mAb as a ligand. The purified allergen was found to be a glycoprotein with a molecular mass of 26 kDa. During the purification process the allergen was converted to more acidic proteins with the same molecular mass, suggesting that the allergen is unstable. The sugar composition and amino acid sequence of Gly m Bd 28K suggest that the allergen is a new glycoprotein with an Asn-linked sugar moiety. The distribution of the allergen in soybean products was examined by an immunoblotting technique with the mAb.

Purification and Characterization of Soybean Allergen Gly m Bd 28K

By a sandwich enzyme-linked immunosorbent assay, a soybean major allergen, Gly m Bd 30K, in soybean products was measured The allergen occurred at high concentrations in soy milk, tofu, kori-dofu, and yuba, but its content in kinako was small No allergen was found in fermented foods such as miso, shoyu, and natto The allergen was clearly shown to occur in meat balls, beef croquettes, and fried chicken that contained soybean protein isolate

Measurement of Gly m Bd 30K, a Major Soybean Allergen, in Soybean Products by a Sandwich Enzyme-linked Immunosorbent Assay

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