دانلود رایگان مقاله لاتین تصفیه کاناوانین از سایت الزویر
عنوان فارسی مقاله:
تصفیه کاناوانین از سبزی نرم برگ ماشک
عنوان انگلیسی مقاله:
Purification of canavanine from the legume Vicia disperma
سال انتشار : 2016
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مقدمه انگلیسی مقاله:
1. Introduction
Vicia disperma DC. (Fabaceae), also known as two-seeded vetch, is a drought-resistant, annual climbing legume with stems up to one meter long. Fruits are very abundant and have one or two seeds, usually two. V. disperma is very common in the Mediterranean Region, especially in the Iberian Peninsula, Italy, south of France, and northern Africa. Nevertheless, and despite its high fruit yield and good agronomic properties, there are no reports on the use of this legume as food or animal feed. Previous studies in our laboratory showed that V. disperma seeds are rich in polyphenols with high antioxidant activity, and contain protein and fatty acids with good nutritional value (Pastor-Cavada et al., 2011a, 2011b, 2009). Plants produce and accumulate different types of secondary compounds, including glucosinolates, alkaloids, polyphenols, essential oils, and free amino acids, which in many cases have a defensive role against predators. Many legumes, including legume crops, accumulate significant amounts of free amino acids in their seeds. Canavanine is a non-protein amino acid present in many legumes, such as Canavalia, Dioclea, Colutea, and Robinia (Rosenthal, 2001), and in several Vicia species including V. disperma (Bell and Tirimanna, 1965). Canavanine is an arginine analog with antinutritional activity as an antimetabolite that is incorporated into proteins of the predator substituting for arginine (Rosenthal, 1977a), leading to deficient protein conformations with loss of functionality (Rosenthal, 2001). Nevertheless, canavanine also has some activities with potential health promoting and even therapeutic potential. Thus, canavanine inhibits the growth of colon tumors (Thomas et al., 1986), and in combination with low levels of arginine induces apoptosis in a number of cancerous cells (Vynnytska et al., 2011, 2012; Bence et al., 2002; Jang et al., 2002). The antiproliferative activity of the legume Sutherlandia frutescens has been attributed at least partially to its content in canavanine (Van Wyk and Albrecht, 2008). Canavanine also has antiviral activity as reviewed in Bell et al. (2008), and potential health promoting or therapeutic properties by inhibiting nitric oxide synthase (Teale and Atkinson, 1994). Although there are studies on the free amino acid composition in species belonging to the Fabaceae family reporting the presence of canavanine (Bell and Tirimanna, 1965; Bell et al., 1978), the inter-population variability, and quantification of this amino acid in V. disperma seeds, as well as its purification from these seeds, have not been previously investigated. While large amounts of free amino acids are used by the pharmaceutical, cosmetic, agricultural, and feed and food industries, the nutrition and health products industries are the mayor consumers of free amino acids driving the search for new production and purification methods. Although fermentation, protein hydrolysis, chemical synthesis, and enzymatic catalysis are the traditional methods for production of amino acids (Leuchtenberger et al., 2005), plants represent “green sources” of amino acids with a great potential. The goal of the present research was to analyze canavanine in seeds collected from a number of V. disperma populations in southern Spain and to explore purification methods in order to determine whether V. disperma represents a potential source of this amino acid.
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کلمات کلیدی:
Purification and properties of argininosuccinate ... - ACS Publications pubs.acs.org/doi/abs/10.1021/bi00545a015 by ME Kimball - 1980 - Cited by 16 - Related articles Feb 1, 1980 - Purification and properties of argininosuccinate synthetase from normal and canavanine-resistant human lymphoblasts. Margaret E. Kimball ... Purification and properties of argininosuccinate synthetase ... - NCBI www.ncbi.nlm.nih.gov/pubmed/6766737 Biochemistry. 1980 Feb 19;19(4):705-9. Purification and properties of argininosuccinate synthetase from normal and canavanine-resistant human lymphoblasts. Purification and characterization of the higher plant enzyme L ... https://www.ncbi.nlm.nih.gov › NCBI › Literature › PubMed Central (PMC) by GA Rosenthal - 1992 - Cited by 20 - Related articles Mar 1, 1992 - This higher plant is representative of a large number of legumes that synthesize L-canavanine, an important nitrogen-storing nonprotein amino ... Purification and properties of argininosuccinate synthetase ... - NCBI https://www.ncbi.nlm.nih.gov/m/pubmed/6766737 Purification and properties of argininosuccinate synthetase from normal and canavanine-resistant human lymphoblasts. Kimball ME, et al. Biochemistry. 1980. The biochemical basis for L-canavanine tolerance by the tobacco ... www.pnas.org/content/94/6/2255.full.pdf by C Melangeli - 1997 - Cited by 29 - Related articles This communication details purification and characteriza- tion of this canavanine-degrading enzyme, which we have named canavanine hydrolase (CH). THE ENZYMATIC CLEAVAGE OF CANAVANINE TO 0 ... www.jbc.org/content/226/1/485.full.pdf by H Kihara - 1957 - Cited by 25 - Related articles How- ever, cell-free extracts of some strains of S. faecalis do contain a much less active canavanine-destroying enzyme. Partial purification of this enzyme.
