Peanut Arachis hypogaea

Agglutinin (from peanuts) [Arachis hypogaea] [1393-62-0] M, 134,900 (tetramer). Purified... 

Arachidonic acid gets its name from arachidic acid, the saturated C20 fatty acid isolated from peanut (Arachis hypogaea) oil. 

Fig. 5. Water-use efficiency (carbon basis) v. average carbon isotope discrimination in the whole plant, r= -0.88. Open symbols represent well-watered plants and closed symbols represent plants that were droughted. Tifton 8 A, Florunner A, VB187 and +, Chico are cultivars of peanut (Arachis hypogaea). (From Flubick etal., 1986).

Watanabe, T., Akiyama, H., Yamakawa, H., lijima, K., Yamazaki, F., Matsumoto, T., Futo, S., Arakawa, F., Watai, M., and Maitani, T. (2006). A specific qualitative detection method for peanut (Arachis hypogaea) in foods using polymerase chain reaction. /. Food Biochem. 30, 215-233. 

R. Lotan, E. Skutelsky, D. Danon, and N. Sharon, The purification, composition, and specificty of the anti-T lectin from peanut (Arachis hypogaea), J. Biol. Chem., 250 (1975) 8518-8523. 

Arachis (groundnut, peanut) Arachis hypogaea (Leguminosae/ Fabaceae) seed 45-55 oleic (35-72), linoleic (13-43), palmitic (7-16), stearic (1-7), behenic (1-5), arachidic (1-3) food oil, emollient base... 

Stephan, O. and S. Vieths. 2004. Development of a real-time PCR and a sandwich ELISA for detection of potentially allergenic trace amounts of peanut (Arachis hypogaea) in processed foods. JAgric Food Chem 52 (12) 3754-3760. 

Kleber-Janke, T., Crameri, R., Schemer, S., Vieths, S., and Becker, W. 2001. Patient-tailored cloning of allergens by phage display Peanut (Arachis hypogaea) profiling, a food allergen derived from a rare mRNA. J Chromatogr B 756 295-305. 

Peanut (Arachis hypogaea L.) - oil, butter, stearine Pectin... 

Kochert, G., Stalker, H.T., Gimenes, M., Galgaro, L., Lopes, C.R., and Moore, K., RFLP and cytogenetic evidence on the origin and evolution of allotetraploid domesticated peanut, Arachis hypogaea (Legu-minosae), Am. J. Bot., 83, 1282-1291, 1996. 

Hydroxystilbenes such as resveratrol (Figure 29) have been identified in several unrelated families, including the grapevine Vitis vinifera (Vitaceae), peanut Arachis hypogaea (Leguminosae), Veratrum grandifolia... 

Arachis lectin (= Peanut Arachis hypogaea (peanut) [T CCK release T... 

Agglutinin (from peanuts) [Arachis hypogaea] [1393-62-0] M, 134,900 (tetramer). Purified by affinity chromatography on Sepharose- -aminocaproyl-6-D-galactopyranosylamine. [Lotan et al. J Biol Chem 250 8518 1974.]... 

In this contact, some of the medicinal uses of plants were brought to Brazil, above all, by the Portuguese rosemary Rosmarinus officinalis L.), while some of the Indian habits were taken from here to the European and African continents consumption of peanut Arachis hypogaea L.) is an example of this [3]. 

People around the world enjoy Africa s culinary contributions. These include the peanut Arachis hypogaea, Fabaceae), yam (Dioscorea spp., Dioscoreaceae), watermelon Citrullus lanatus, Cucurbitaceae), okra Abelmoschus esculentus, Malvaceae) and many other foods and flavors. In North America and in many other parts of the world there is little recognition of the many contributions that Africa has made to modem culture, i.e., perhaps beyond the domain of etlmobotanists and pharmacognosists. 

Movement of the biological material ricin with soil-size fractions are shown in Figures 4.6 and 4.7. Studies on peanut (Arachis hypogaea) seed lectin show similar results (Zartman et al. 2005). These lectin data are similar in distribution to published values (Ravi et al. 2004). The inhalation of dust generated from ricin-contami-nated soils could pose a serious hazard to war fighters. Work of A. H. Corwin cited in Lamanna (1961) stated that ricin particles with a median diameter of 2 /(ui are 2.75 times as toxic as particles with a maximal particle size of 4.2 pm. 

The peanut Arachis hypogaea) contains a lectin with anti-T (Gal(Pl-3)GalNAc) activity [174]. This antigen appears on human erythrocytes following treatment with sialidase and leads to the phenomenon known as polyagglutinability as monitored by the peanut lectin [175]. Peanut agglutinin, purified by numerous affinity purification schemes, is a tetrameric protein composed of four carbohydrate-free subunits, A/f = 27000Da[176]. The lectin is a metalloprotein rich in acidic and hydroxylic amino acids and devoid of cysteine [176]. 

A recent review by Davis and Rhoades (1994) and an earlier review by Cox, Adams, and Tucker (1982) noted that there have been very few reports of yield increases due to Mo application to peanuts (Arachis hypogaea L.). The earliest report of an increased yield due to Mo application was by Parker (1964), who conducted 15 experiments from 1956 to 1963 in which only one experiment showed a yield increase (31%) due to Mo, which had been applied at a rate of 280 g ha- on a Ruston loamy sand of pH 6.3. Boswell, Anderson, and Welch (1967) conducted 30 Mo experiments on soils whose pH values ranged from 5.0 to 6.8, and they found no increased yields following application of Mo. Sixteen of the experiments were continued for a second year, with no significant yield increases. They had only one experiment in which the method and timing of application had an effect on yield. They found that the combination of seed treatment and foliar application of Mo at 3 weeks after early bloom was superior to foliar application at 6 weeks after early bloom. 

Roasted peanuts (Arachis hypogaea) possess a unique emd widely enjoyed flavor. In this review we will cover the formation of peanut flavor volatiles, analytical aspects, sensory analysis emd correlation of Instrumental and sensory results. 

Basha, S.M. and Young, C.T., Changes in the polypeptide composition of peanut (Arachis hypogaea L.) seed during oil roasting, J. Agric. Food Chem., 33, 350-354, 1985. 

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