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MeSH Review

Arachis hypogaea

 
 
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Disease relevance of Arachis hypogaea

  • The specimens incubated with saline, fibronectin, ADP, and arachis oil were examined histologically; with the exception of arachis oil all displayed ectodermal epithelial and mesenchymal hyperplasia of the membrane in association with increased vascularity [1].
  • Isolation and characterization of symbiotic mutants of bradyrhizobium sp. (Arachis) strain NC92: mutants with host-specific defects in nodulation and nitrogen fixation [2].
  • The rats were given BHA at a dose level of 2% in a powdered diet or by oral intubation of 1 g BHA/kg body weight/day in arachis oil [3].
  • Four of 14 strains of Rhizobium japonicum from soybean nodulated peanut (Arachis hypogaea L. cultivar Jumbo Virginia), and 3 of 8 Rhizobium sp. strains from peanut nodulate soybean (Glycine max (L.) Merr. cultivar Harosoy 63) [4].
  • One hundred thirty-two patients with breast cancer were examined for exposure of cryptantigens on their erythrocytes (RBC) using a lectin panel consisting of Arachis hypogaea and Glycine soja [5].
 

High impact information on Arachis hypogaea

  • Alterations in the binding pattern between paraffin and frozen sections were noted only for Arachis hypogaea and Glycine max [6].
  • We recently reported that Arachis hypogaea serine/threonine/tyrosine (STY) protein kinase is developmentally regulated and is induced by abiotic stresses (Rudrabhatla, P., and Rajasekharan, R. (2002) Plant Physiol. 130, 380-390) [7].
  • The enzyme was purified by successive chromatographic separations on octyl-Sepharose, blue-Sepharose, Superdex-75, and palmitoyl-CoA-agarose to apparent homogeneity from developing peanut (Arachis hypogaea) cotyledons [8].
  • The two amino acid motifs in the chalcone synthase from Pinus sylvestris (Gln-Gln) and in the stilbene synthases from P. sylvestris (Gln-His) and Arachis hypogaea (His-Gln) were changed by site-directed mutagenesis into all sequence combinations as found in the natural enzymes [9].
  • This pattern contrasts with the detection of the terminal disaccharide galactose beta-1,3-N-acetylgalactosamine by Arachis hypogaea lectin in middle and trans-Golgi compartments, which are considered elongation sites for O-glycosylation [10].
 

Chemical compound and disease context of Arachis hypogaea

 

Biological context of Arachis hypogaea

 

Anatomical context of Arachis hypogaea

 

Associations of Arachis hypogaea with chemical compounds

  • A comparison between the carbohydrate-binding specificities of amaranthin and peanut (Arachis hypogaea) agglutinin is discussed [26].
  • A 4-methylene-L-glutamine amidohydrolase has been partially purified from leaf extracts of 2-week germinated peanuts (Arachis hypogaea) [27].
  • For histochemical localization of sialic acid, paraffin sections were treated with Arachis hypogaea lectin (PNA) before and after neuraminidase treatment [28].
  • Formalin-fixed, paraffin-embedded tissues were tested with Glycine maximus (SBA), Dolichos biflorus (DBA), Triticum vulgaris (WGA), Concanavalia ensiformis (Con A), Lotus tetragonolobus (LTA), Arachis hypogaea (PNA), and Bandeiraea simplicifolia (BSAI) [29].
  • Control experiments with neuraminidase-treated brain samples revealed positivity to the lectin from Arachis hypogaea (PNA), which is specific for galactose [30].
 

Gene context of Arachis hypogaea

  • They were all labeled by peanut lectin (Arachis hypogaea) and three showed reactivity for S-100 protein [31].
  • Signaling by glutamate dehydrogenase in response to pesticide treatment and nitrogen fertilization of peanut (Arachis hypogaea L.) [32].
  • Addition of the carbohydrates methyl alpha-D-mannopyranoside and methyl alpha-D-galactopyranoside to the interaction medium, pretreatment of Lec1 and Lec2 cells with lectins Concanavalina A and Arachis hypogaea and pretreatment with sodium periodate decreased the adhesion and the endocytic index [33].
  • The glycoprotein CEA (carcinoembryonic antigen) carries carbohydrate groups, which react with the plant lectins from Agaricus bisporus, Arachis hypogaea (peanut), with Tridacnin from invertebrate clams and with the anti-A lectins from snails [34].
  • Pancreatic gp58 was susceptible to alpha-N-acetylgalactosaminidase digestion and it bound concanavalin A, Helix pomatia, Dolichos biflorus, soybean agglutinin, and Bauhinia purpurea lectins, but not Ricinus communis agglutinin or lectins from Griffonia simplicifolia-1, Arachis hypogaea, and Limulus polyphemus [35].
 

Analytical, diagnostic and therapeutic context of Arachis hypogaea

  • Release evoked by electrical stimulation (difference between stimulated and resting release) in the absence of atropine, i.e., "basal rate," for strips taken at various times after a single injection of DFP did not differ from that for strips from animals receiving arachis oil only [36].
  • The dose of chlormethiazole was such that it produced the same degree of hypnosis as would be expected from oral administration of two capsules each containing 192 mg of base in arachis oil [37].
  • The IUD stimulated a deciduomal response in every animal, whereas the traumatization with arachis oil had no such effect; the variation in the peripheral and utero-ovarian steroid levels could not explain the variation in the incidence of the deciduomal reaction [38].
  • Chick bioassay of available methionine and sulphur amino acids (SAA). Assay of African oil bean meal (Pentaclethra macrophylla Benth), conophor seed meal (Tetracarpidium conophorum, Hutch) and groundnut meals (Arachis hypogeae Linn) [39].
  • A glucose-specific lectin has been purified to apparent homogeneity from 7-day-old peanut (Arachis hypogaea) roots by affinity chromatography on a Sephadex G-50 [40].

References

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  3. Effects of BHA and related phenols on the forestomach of rats. Altmann, H.J., Grunow, W., Mohr, U., Richter-Reichhelm, H.B., Wester, P.W. Food Chem. Toxicol. (1986) [Pubmed]
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  16. Synthesis of N,N'-bis(acrylamido)acetic acid-based T-antigen glycodendrimers and their mouse monoclonal IgG antibody binding properties. Roy, R., Baek, M.G., Rittenhouse-Olson, K. J. Am. Chem. Soc. (2001) [Pubmed]
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