Search PubMed⌕ Search

SEARCH · Search PubMed

Results for “peanut”

Search indexed PubMed citations on genomics, clinical trials, systematic reviews and public health. Explore titles, authors and supplied subject terms, then open the PubMed record.

Quote a phrase for an exact phrase match. Source license links do not imply unrestricted reuse.

At least 559 records · Page 31Linked to original sources
PubMedDate not supplied

Detection and determination of theobromine and caffeine in urine after administration of chocolate-coated peanuts to horses.

The objective of this study was to determine the urinary excretion of methylxanthines in horses following ingestion of chocolate over eight days. The study was performed in response to gas chromatography-mass spectrometry (GC-MS) confirmation of the presence of caffeine in a positive urine test in a racehorse. The trainer of the horse alleged that he often administered chocolate-coated peanuts as treats to his horses, and he believed that the ingestion of chocolate was responsible for the positive urine test. The urinary excretion of theobromine and caffeine after the ingestion of chocolate-coated peanuts was investigated in three horses. Enzyme-linked immunoassay (ELISA), high-performance liquid chromatography (HPLC), and GC-MS assays were performed on all urine specimens. Theobromine (HPLC) was detected for 72 h and caffeine (GC-MS) for 48 h after chronic ingestion of chocolate-coated peanuts. Methylxanthines were detected by ELISA for 120 h after administration of chocolate.

Animal Feed↗
PubMedDate not supplied

The phylogenetic relationship of possible progenitors of the cultivated peanut.

The cultivated peanut (Arachis hypogaea L.) is an allotetraploid composed of A and B genomes. The phylogenetic relationship among the cultivated peanut, wild diploid, and tetraploid species in the section Arachis was studied based on sequence comparison of stearoyl-ACP desaturase and oleoyl-PC desaturase. The topology of the trees for both fatty acid desaturases displayed two clusters; one cluster with A genome diploid species and the other with B genome diploid species. The two homeologous genes obtained for each of the two fatty acid desaturases from the tetraploid species A. hypogaea and A. monticola were separated into the A and B genome clusters, respectively. The gene phylogenetic trees showed that A. hypogaea is more closely related to the diploid species A. duranensis and A. ipaensis than to the wild tetraploid species A. monticola, suggesting that A. monticola is not a progenitor of the cultivated peanut. In addition, for the stearoyl-ACP desaturase, the A. duranensis sequence was identical with one of the sequences of A. hypogaea and the A. ipaensis sequence was identical with the other. These results support the hypothesis that A. duranensis and A. ipaensis are the most likely diploid progenitors of the cultivated tetraploid A. hypogaea.

Amino Acid Sequence↗
PubMed1983

Comparative vitamin B-6 bioavailability from tuna, whole wheat bread and peanut butter in humans.

Relative bioavailability of vitamin B-6 from tuna, whole wheat bread and peanut butter was investigated in eight men. The study was divided into a 10-day adjustment and three, 14-day experimental periods in a 3 X 3 Latin square design. Vitamin B-6 intake was set at 1.6 mg/day, with 50% of the intake coming from one of the three experimental foods and 50% from a basal diet. Daily complete urine and fecal collections were made. Urine was analyzed for 4-pyridoxic acid (4PA) and vitamin B-6, fecal samples for vitamin B-6 and plasma (sampled every 5 days) for pyridoxal 5'-phosphate (PLP). Mean values +/- SD for the adjustment, tuna, whole wheat bread and peanut butter periods were: 5.65 +/- 1.76, 4.89 +/- 1.10, 3.62 +/- 0.66 and 2.80 +/- 0.50 mumol/day for 4-pyridoxic acid; 0.98 +/- 0.34, 1.05 +/- 0.20, 0.76 +/- 0.09 and 0.68 +/- 0.19 mumol/day for urinary vitamin B-6; 2.72 +/- 0.94, 3.08 +/- 0.73, 3.80 +/- 0.78 and 4.42 +/- 1.03 mumol/day for fecal vitamin B-6 and 65.0 +/- 23.30, 64.8 +/- 29.80, 49.3 +/- 14.40 and 48.4 +/- 20.20 nM for plasma pyridoxal 5'-phosphate, respectively. 4PA and urinary vitamin B-6 excretion were significantly (P less than or equal to 0.01) higher in the tuna period than in either the whole wheat bread or peanut butter periods.(ABSTRACT TRUNCATED AT 250 WORDS)

Adult↗
PubMed1988

65Copper absorption by women fed intrinsically and extrinsically labeled goose meat, goose liver, peanut butter and sunflower butter.

Absorption of stable 65Cu incorporated intrinsically or extrinsically into foods was studied in women fed a diet marginal in Cu content. Isotopic enrichment was 73.1 +/- 1.0 atom percent 65Cu in goose breast meat, 74.9 +/- 0.5 atom percent in goose liver, and 55-69.5 atom percent in two crops of peanuts. Seven women were fed a basal diet containing 1.25 mg Cu/d. At 4-wk intervals, they were fed test meals over a 3-d period; each set of meals contained one of the labeled test foods in amounts with similar copper content. Absorption of 65Cu from intrinsically labeled liver was (mean +/- SD) 65 +/- 4%; extrinsic liver, 65 +/- 10%; E/I = 1.00 +/- 0.16. 65Cu absorption from intrinsically labeled goose breast meat was 54 +/- 6%; extrinsic meat, 52 +/- 10%; E/I = 0.97 +/- 0.18. 65Cu absorption from intrinsically labeled peanut butter was 58 +/- 15%; extrinsic peanut butter, 54 +/- 10%; E/I = 0.93 +/- 0.11. 65Cu absorption from extrinsically labeled sunflower butter was 50 +/- 2%. There were no differences in absorption of intrinsic and extrinsic Cu from these foods. Absorption of Cu was significantly higher from goose liver than from goose meat or sunflower butter (P less than 0.05). With a dietary intake of 1.25 +/- 0.20 mg Cu/d, Cu balance, exclusive of surface losses, was essentially zero (0.01 +/- 0.13 mg/d) in the seven subjects.

Animals↗
PubMed1997

Microbial phytase improves amino acid utilization in young chicks fed diets based on soybean meal but not diets based on peanut meal.

Studies were conducted to evaluate the ability of supplemental microbial phytase to improve performance of young chicks fed phytate-containing, amino acid-deficient diets. Diets based on corn and peanut meal or soybean meal (SBM) and dextrose were fed to young chicks housed in battery cages for 10- and 13-d experimental periods. Assays were designed to evaluate phytase supplementation of both amino acid-deficient and amino acid-adequate diets. Weight gain, feed intake, and gain:feed values of chicks increased (P < 0.05) when deficient amino acids were serially supplemented to either the corn-peanut meal or SBM-dextrose diets. Phytase supplementation (600 and 1,200 U/kg) to the corn-peanut meal diet resulted in no significant differences in weight gain, feed intake, or gain:feed values of chicks when the diet was either deficient or adequate in amino acids. However, phytase supplementation (1,200 U/kg) produced significant increases (P < 0.05) in gain:feed values, but not weight gain, of chicks when they were fed the amino acid-deficient, but not the amino acid-adequate, SBM-dextrose diet. This gain:feed response to phytase supplementation of the amino acid-deficient SBM-dextrose diet occurred in both crossbred (New Hampshire x Columbian) and commercial (Ross x Hubbard) chicks. A digestibility assay was also performed using cecectomized roosters fed dehulled SBM containing three levels of phytase (0, 600, and 1,200 U/kg). When averaged across nine essential amino acids and cystine, true amino acid digestibility (TAAD) values were increased by approximately 2% when 1,200 U/kg phytase was included with SBM and administered to cecectomized roosters. However, neither TAAD values nor TMEn were significantly improved by the phytase addition.

6-Phytase↗
PubMed1994

Peanut butter and fatal fluoride poisoning. A case of mistaken identity.

We report here a case of an adult seeking a late night peanut butter snack who mistook for peanut butter a fluoride containing glass etching compound. The glass etching compound was of a color and consistency similar to peanut butter and was packaged in a similar appearing container. The decedent survived for six hours after the fluoride ingestion. He was admitted to the emergency room in stable condition with severe gastrointestinal symptoms. His condition deteriorated rapidly prior to death with abrupt cardiac arrest and profound hypocalcemia (5.5 mg/dl). Autopsy showed only gastric hyperemia and discoloration with a postmortem blood fluoride level of 19 mg/L.

Arachis↗
PubMed1994

A Peanut Nodule Lectin in Infected Cells and in Vacuoles and the Extracellular Matrix of Nodule Parenchyma.

Root nodules on peanut (Arachis hypogaea L.) accumulate a galactose/lactose-binding lectin that is similar, but not identical, to the major seed lectin in peanut. The function of the peanut nodule lectin (PNL) is not known. In the current study, we have investigated the location of lectin in the nodule using immunogold labeling and enzyme-linked immunosorbant assays (ELISA). Lectin was most abundant in the nodule parenchyma, where it accumulated in vacuoles, suggesting a possible role as a vegetative storage protein. Lectin was also detected in the extracellular matrix in the nodule parenchyma, a location that corresponds to the tissue layer forming a barrier to oxygen diffusion. The potential for interactions between PNL and other cell wall components, including a previously described high-molecular weight glycoprotein that co-localizes with PNL, is discussed. Within infected cells, lectin was not detectable by immunogold labeling within the cytoplasm, but light labeling was suggestive of lectin localization within the symbiosome lumen. Analysis of fractionated symbiosomes by the more sensitive ELISA technique confirmed that lectin was present within the symbiosome, but was not bound to bacteroids. Our results indicate that PNL probably plays several roles in this nitrogen-fixing symbiosis.

Journal Article↗
PubMed1967

Isolation and characterization of peanut spherosomes.

Spherosomes of cotyledons of germinating peanuts (Arachis hypogea L.) were examined by electron microscopy and found to be particles about 1.0 to 2.0 mu in diameter bounded by a limiting membrane. Isolated spherosomes appear similar to spherosomes in situ. The isolated spherosomes are composed of 98.1% total lipids, 0.77% phospholipid and 1.27% protein by dry weight. The amounts of protein and phospholipid associated with the isolated spherosomes are sufficient to account for limiting membranes. Spherosomes amply account for the lipid in a peanut cotyledon. The activity of lipase and fatty acyl-Coenzyme A synthetase is not associated with the isolated spherosomes. This suggests that peanut spherosomes are principal sites of lipid storage but not of lipid degradation.

Journal Article↗
PubMed1969

Movement and Fate of p-Nitrophenyl-alpha,alpha,alpha-Trifluoro-2-Nitro-p Tolyl Ether-1'-C in Peanut Seedlings.

Autoradiographs and liquid scintillation counts of peanut (Arachis hypogaea L., var. Starr) seedlings indicate that p-nitrophenyl-alpha,alpha,alpha-trifluoro-2-nitro-p-tolyl ether-1'-(14)C (C-6989) is rapidly absorbed from nutrient solution but only 6.5% of the radioactivity absorbed is translocated to the shoot after 144 hr, with the acropetal movement being confined to the stem and petiole.Metabolism of C-6989 by peanut seedlings proceeds rapidly, the major pathway being hydrolysis of the ether linkage and reduction of the 4-nitrophenol formed to 4-aminophenol. After 48 hr 4-aminophenol, C-6989 and 4-nitrophenol comprised 67.8, 17.4, and 13.5% of the total radioactivity recovered, respectively. After 144 hr these compounds comprised 94.3, 4.0, and 0.9% of the radioactivity, respectively.Reduction of one of the nitro groups of C-6989 followed by hydrolysis of the ether linkage is a minor pathway of metabolism in peanut seedlings. Small amounts (less than 1.0% of the total radioactivity) of both p-mitrophenyl-alpha,alpha,alpha-trifluoro-2-amino-p-tolyl ether and p-amino-phenyl-alpha,alpha,alpha-trifluoro-2-nitro-p-tolyl ether were present but no p-aminophenyl-alpha,alpha,alpha-trifluoro-2-amino-p-tolyl ether was detected. Two very minor metabolites (less than 0.1% of the radioactivity) were detected which were not identified. These metabolites were possibly conjugates of the phenol derivatives with natural plant constituents, or products of substitution on, or ring cleavage of, the phenols.

Journal Article↗
PubMed1969

Respiratory changes during seed germination. Histological distribution of respiratory enzymes and mobilization of fat reserves in castor bean endosperm and peanut cotyledons.

Germinating peanut cotvledons and germinating castor bean endosperm have been compared with respect to their rates of fat dissimilation and with respect to the anatomical distribution of respiratory activity. The lipid mobilization is much slower in peanut cotyledons than in castor bean endosperm. Light has essentially no effect on either system. As germination progresses, the majority of the succinic dehydrogenase and cytochrome oxidase activities become localized in the vein regions of peanut cotyledons. In the castor bean endosperm these two activities are uniformly distributed throughout the storage parenchyma and increase with germination until the organ becomes soft and visibly senescent.

Arachis↗
PubMed1970

The development of glyoxysomes in peanut cotyledons and maize scutella.

The development of glyoxysomes during germination has been studied in isolated peanut (Arachis hypogaea L.) cotyledons and in maize (Zea mays L.) scutella. In peanut cotyledons isocitratase, malate synthetase, and protein associated with the glyoxysomal fraction increase simultaneously from the 3rd to the 8th day of incubation. In scutella of germinating maize seeds the specific activities of isocitratase, malate synthetase, and catalase associated with the glyoxysomes rise until the 4th day of germination and then decline while the total amount of protein present in the fraction stays constant during the first 5 days. If the peanut cotyledons are cultured in 2% glucose, the development of isocitratase and malate synthetase is severely inhibited, but the level of the glyoxysomal protein is not measurably affected.

Arachis↗
PubMed1972

Physiology of Oil Seeds: IV. Role of Endogenous Ethylene and Inhibitory Regulators during Natural and Induced Afterripening of Dormant Virginia-type Peanut Seeds.

To further elucidate the regulation of dormancy release, we followed the natural afterripening of Virginia-type peanut (Arachis hypogaea L.) seeds from about the 5th to 40th week after harvest. Seeds were kept at low temperature (3 +/- 2 C) until just prior to testing for germination, ethylene production, and internal ethylene concentration. Germination tended to fluctuate but did not increase significantly during the first 30 weeks; internal ethylene concentrations and ethylene production remained comparatively low during this time. When the seeds were placed at room temperature during the 30th to 40th weeks after harvest, there was a large increase in germination, 49% and 47% for apical and basal seeds, respectively. The data confirm our previous suggestion that production rates of 2.0 to 3.0 nanoliters per gram fresh weight per hour are necessary to provide internal ethylene concentrations at activation levels which cause a substantial increase of germination. Activation levels internally must be more than 0.4 microliter per liter and 0.9 microliter per liter for some apical and basal seeds, respectively, since dormant-imbibed seeds containing these concentrations did not germinate. Abscisic acid inhibited germination and ethylene production of afterripened seeds. Kinetin reversed the effects of ABA and this was correlated with its ability to stimulate ethylene production by the seeds. Ethylene also reversed the effects of abscisic acid. Carbon dioxide did not compete with ethylene action in this system. The data indicate that ethylene and an inhibitor, possibly abscisic acid, interact to control dormant peanut seed germination. The inability of CO(2) to inhibit competitively the action of ethylene on dormancy release, as it does other ethylene effects, suggests that the primary site of action of ethylene in peanut seeds is different from the site for other plant responses to ethylene.

Journal Article↗
PubMed1979

Distribution of Lectins in the Jumbo Virginia and Spanish Varieties of the Peanut, Arachis hypogaea L.

Peanut lectin was purified from seed meal of the Spanish and Jumbo Virginia varieties of peanut (Arachis hypogaea L.) by affinity chromatography on lactose coupled to Sepharose 4B. Polyacrylamide gel isoelectric focusing resolved the lectin preparation from Jumbo Virginia seeds into seven isolectins (pI 5.7, 5.9, 6.0, 6.2, 6.3, 6.5, and 6.7). Seed meal from the Spanish variety contained six isolectins which were indistinguishable from the pI 5.7, 5.9, 6.2, 6.3, 6.5, and 6.7 isolectins from Jumbo Virginia. Quantitative, lactose-specific hemagglutination was used to examine the lectins in tissues of both peanut varieties. In young (3- to 9-day-old) seedlings of each variety, more than 90% of the total amount of lectins detected in the plants was in the cotyledons. Most of the remainder was in hypocotyls, stems, and leaves; young roots contained no more than 4 micrograms of lectin per plant. Lectins were present in all nonroot tissues of 21- to 30-day-old seedlings, except 27-day-old Spanish hypocotyls. As cotyledons of each variety senesced, several of the more basic isolectins decreased to undetectable levels, but the acidic isolectins remained until at least 15 days after planting. Some of the seed isolectins and several apparently new lactose-binding lectins were also identified in affinity-purified extracts of 5-day-old roots and hypocotyls. Rabbit antibodies raised against the Jumbo Virginia seed isolectin preparation reacted with seed, cotyledon, and hypocotyl lectin preparations from both varieties. Analysis of seed lectin preparations from seven varieties of A. hypogaea and of a related species (A. villosulicarpa) indicated that isolectin composition in Arachis may be a characteristic of both the species and the subspecies (botanical type) to which the variety belongs.

Journal Article↗
PubMed1981

4-methyleneglutamine in peanut plants: dynamics of formation, levels, and turnover in relation to other free amino acids.

Neither 4-methyleneglutamine nor 4-methyleneglutamic acid were found in free or bound form in ungerminated peanut seeds (Arachis hypogaea L.). Both, however, were formed soon after germination; whereas, 4-methyleneglutamic acid appeared slightly before 4-methyleneglutamine, the former remained at a low concentration while the level of 4-methyleneglutamine rose rapidly between 2 and 10 days of germination and declined slowly thereafter. Free proline and glutamine followed a pattern similar to 4-methyleneglutamine; on the other hand, asparagine increased for at least 20 days but other free amino acids remained at relatively low, constant levels. In mature peanut plants, 4-methyleneglutamine occurred in all parts except developing pods, was virtually the only free amino acid in xylem sap, and constituted about 70% of the total soluble nitrogen of sap. In contrast, 4-methyleneglutamic acid was found only in leaves and stems in highly variable amounts.Levels of 4-methyleneglutamine were largely independent of the processes of nodulation and nitrogen fixation. This amide was degraded much more slowly in nitrogen-deficient plants than were any of the other free amino acids and did not become labeled when a photosynthesizing plant was exposed to (14)CO(2) for 24 hours. The results indicate that 4-methyleneglutamine is the principle carrier of nitrogen in the xylem of peanut plants but its carbon skeleton appears to turn over very slowly.

Journal Article↗
PubMed1982

Ethylene Production and Leaflet Abscission of Three Peanut Genotypes Infected with Cercospora arachidicola Hori.

Ethylene can induce abscission of leaves and other plant organs. Increased ethylene production by plant tissues can occur after invasion by microorganisms. The fungus Cercospora arachidicola Hori, attacks peanut leaflets and causes defoliation. Our objective was to determine if ethylene was involved in this defoliation. Leaves of three peanut, Arachis sp., genotypes were inoculated with C. arachidicola. Two genotypes, ;Tamnut 74' and PI 109839, produced ethylene and were defoliated. The third genotype, PI 276233, a wild species, did not produce ethylene above control levels and was not defoliated. Increase in ethylene production by Tamnut 74 and PI 109839 coincided with appearance of disease symptoms. Tamnut 74 produced the most ethylene, but PI 109839 was equally defoliated. Thus, less overall ethylene production did not necessarily indicate a more resistant genotype in this system unless ethylene production remained at control levels, as it did for PI 276233. Ethylene sufficient to initiate abscission could have been produced by the seventh day after inoculation when it was similar for both Tamnut 74 and PI 109839, but 3 to 4 times control amounts. This occurred before the rapid increase in ethylene production and before disease symptoms were visible. Silver ion, a potent inhibitor of ethylene action, was sprayed at three concentrations on intact Tamnut 74 plants. All rates reduced abscission and 150 mg/liter Ag(I) decreased abscission to below 10%. The data indicate that ethylene produced by peanut leaves in response to C. arachidicola infection initiates abscission and that ethylene action can be blocked by Ag(I) in such a host-pathogen interaction.

Journal Article↗
PubMed1984

Inhibition by auxins of 4-methyleneglutamic Acid synthesis in tissue cultures of peanut seeds.

Callus cultures of peanut (Arachis hypogaea L. cv Valencia Tennessee Red) cotyledons grown on Linsmaier and Skoog medium containing normal levels of auxin and cytokinin do not synthesize either 4-methyl-eneglutamic acid or 4-methyleneglutamine, which nonprotein amino acids are normally found in significant amounts in peanut plants. If mature peanut embryos (with cotyledons removed) are germinated and grown on a similar medium containing no added phytohormone, normal levels of these two amino acids accumulate. The addition of an auxin, however, prevents formation of 4-methyleneglutamic acid and 4-methyleneglutamine; typical levels of other free amino acids are seen and excised embryos so cultured develop into apparently otherwise normal plants. Kinetin addition to embryo cultures has little or no effect. 4-Methyleneglutamine is formed when 4-methyleneglutamic acid is added to embryo cultures maintained on auxin-containing medium, indicating that the phytohormone does not block amidation but rather the biosynthesis of 4-methyleneglutamic acid.

Journal Article↗
PubMed1991

4-methyleneglutamine amidohydrolase from peanut leaves : preparation, catalytic properties, and immunological responses of a highly purified form of the enzyme.

4-Methyleneglutamine amidohydrolase has been extracted and purified over 1000-fold from 14-day-old peanut (Arachis hypogaea) leaves by modification of methods described previously. The purified enzyme shows two bands of activity and three to four bands of protein after electrophoresis on nondenaturing gels. Each of the active bands is readily eluted from gel slices and migrates to its original position on subsequent electrophoresis. Although they are electrophoretically distinct, the two forms of the enzyme are immunologically identical by Ouchterlony double-diffusion techniques and have similar catalytic properties. Activity toward glutamine that has a threefold lower V(max) and a four-fold higher K(m) value copurifies with MeGln aminohydrolase activity. 4-Methyleneglutamine and 4-methyleneglutamic acid inhibit the hydrolysis of glutamine while glutamine inhibits 4-methyleneglutamine hydrolysis, further indicating the identity of the activity toward both substrates. Amidohydrolase activity is stimulated up to threefold by preincubation with either ionic or non-ionic detergents (0.1%) and also by added proteins (0.5% bovine serum albumin or whole rabbit serum); it is inhibited 50% by 1 millimolar borate or the glutamine analog, albizziin (10 millimolar). Rabbit antiserum to the purified peanut enzyme cross-reacts with one or more proteins in extracts of some plants but not others; in no instance, however, was 4-methyleneglutamine amidohydrolase activity detected in other species. Overall, the results support the hypothesis that 4-methyleneglutamine supplies N, via its hydrolysis by the amidohydrolase, to the growing shoots of peanut plants, whereas glutamine hydrolysis is prevented by the prepon-derance of the preferred substrate. Some results also suggest that this amidohydrolase activity may be regulated by metabolites and/or by association with other cellular components.

Journal Article↗
PubMed2001

The combination of molecular dynamics with crystallography for elucidating protein-ligand interactions: a case study involving peanut lectin complexes with T-antigen and lactose.

Peanut lectin binds T-antigen [Galbeta(1-3)GalNAc] with an order of magnitude higher affinity than it binds the disaccharide lactose. The crystal structures of the two complexes indicate that the higher affinity for T-antigen is generated by two water bridges involving the acetamido group. Fresh calorimetric measurements on the two complexes have been carried out in the temperature range 280-313 K. Four sets of nanosecond molecular-dynamics (MD) simulations, two at 293 K and the other two at 313 K, were performed on each of the two complexes. At each temperature, two somewhat different protocols were used to hydrate the complex in the two runs. Two MD runs under slightly different conditions for each complex served to assess the reliability of the approach for exploring protein-ligand interactions. Enthalpies based on static calculations and on MD simulations favour complexation involving T-antigen. The simulations also brought to light ensembles of direct and water-mediated protein-sugar interactions in both the cases. These ensembles provide a qualitative explanation for the temperature dependence of the thermodynamic parameters of peanut lectin-T-antigen interaction and for the results of one of the two mutational studies on the lectin. They also support the earlier conclusion that the increased affinity of peanut lectin for T-antigen compared with that for lactose is primarily caused by additional water bridges involving the acetamido group. The calculations provide a rationale for the observed sugar-binding affinity of one of the two available mutants. Detailed examination of the calculations point to the need for exercising caution in interpreting results of MD simulations: while long simulations are not possible owing to computational reasons, it is desirable to carry out several short simulations with somewhat different initial conditions.

Anti-Bacterial Agents↗