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PubMed1985

The binding of peroxidase-labelled lectins to human breast epithelium. IV--The reactivity of breast carcinomas to peanut, soy bean and Dolichos biflorus agglutinins.

The binding of the lectins from peanut, soy bean and Dolichos biflorus (specific for galactose and/or N-acetyl-D-galactosamine), to human breast carcinomas has been investigated. In contrast to the consistent pattern found in normal breast the reactivity of carcinomas to peanut lectin is varied, the most striking differences being prominent binding without desialation in some tumours and virtual lack of reactivity in others. There tends to be a greater degree of binding of soy bean agglutinin to carcinomas than normal although this is not absolute, and the reverse applies to Dolichos biflorus agglutinin. Comparison of the binding of the three lectins has revealed a complex heterogeneity of the carbohydrate chains within individual tumours and between different carcinomas. A significant relationship between peanut lectin binding, with the use of neuraminidase, and tumour differentiation as been found, and to a lesser extent with soy bean agglutinin when desialation is performed. However, the pattern of reactivity of the carcinomas with these three lectins does not appear to be related to local lymph node metastasis.

Arachis↗

PubMed1982

Ultrastructural visualization of galactose in the glycoprotein of gastric surface cells with a peanut lectin conjugate.

The ultrastructural localization of peanut lectin-binding sites in the gastric surface epithelial cell has been studied using a horseradish peroxidase-labelled peanut lectin (PL-HRP) conjugate and other cytochemical techniques. The PL-HRP procedure has visualized glycoprotein with presumed terminal galactose residues in the apical plasmalemma and secreted mucins and has localized such glycoprotein selectively in the 'intermediate Golgi cisternae' situated between the saccules of the maturing face and those of the forming face of the Golgi stacks. Other cytoplasmic organelles, including the forming and stored secretory granules, did not reveal glycoprotein with terminal galactosyl residues. These results demonstrate the applicability of the PL-HRP labelling technique at the electron microscopical level to localize not only extra but also intracellular peanut lectin-reactive sites. The observation afford information concerning the possible site in the Golgi apparatus where galactose residues are added to the growing oligosaccharide side-chain of mucous glycoprotein.

Animals↗

PubMed1996

Lectin staining of trichostrongylid nematode eggs of sheep: rapid identification of Haemonchus contortus eggs with peanut agglutinin.

The binding of 10 different lectins to the surface of trichostrongylid nematode eggs of sheep were investigated. Osage orange seed agglutinin bound to eggs from Haemonchus contortus, Ostertagia circumcincta and Trichostrongylus colubriformis, jack bean agglutinin to H. contortus and O. circumcincta eggs and peanut agglutinin to H. contortus eggs only. Staining of egg mixtures with fluorescein-labelled peanut agglutinin showed that the lectin correctly identified the percentage of H. contortus eggs present. Identification of eggs by lectin staining correlated well with results from larval differentiation. The findings suggest that peanut agglutinin can be used in routine diagnostic parasitology for the rapid identification of H. contortus eggs.

Animals↗

PubMed1982

Ultraviolet difference spectroscopy study of peanut lectin binding to Mono- and disaccharides.

Ultraviolet difference spectroscopy was used to study the interaction of peanut (Arachis hypogaea) lectin with complementary carbohydrates. A correlation was observed between variations of ultraviolet spectra during the binding of sugars to the lectin and the specificity and the strength of the binding. The association constant, free energy, enthalpy and entropy for peanut lectin-lactose interactions were calculated over the temperature range 10-30 degrees C. The binding constants for 10 mono- and disaccharides containing a D-galactopyranosyl or a D-talopyranosyl residue were calculated. Comparing their effectiveness to interact with peanut lectin, methyl alpha-D-galactopyranoside appeared to have a more marked affinity than lactose; D-galacturonic acid and methyl 7-deoxy-D-glycero-beta-D-galacto-heptopyranoside had no measurable affinity; the other sugars showed a lower affinity than lactose. The correlations between these differences and the conformations of the sugars obtained by X-ray analysis are discussed.

Binding Sites↗

PubMed1995

[Peanut sensitization and oily solution vitamin preparations].

BACKGROUND AND METHODS: Early sensitization to peanut can occur through milk formulas which contain peanut oil. Thus, the groundnut allergens in relation to the early feeding have been systematically tested in all children referred to the paediatric allergy unit for symptoms not related to peanut allergy. RESULTS: Out of 102 children, 4 to 35 months old, 19 had a positive test (weal > 3 mm). Neither breast feeding nor milk formulas changed the frequency of sensitization. On the contrary, vitamin D preparations in groundnut oil significantly increased the risk (p < 0.008). Odds ratios were 5.47 in the case of neonatal prescription, 4.82 in case of delayed prescription. Odds ratio increased to 8.25 (p < 0.04) in allergic children under two years who had received oily vitamin D preparation during their neonatal period. CONCLUSIONS: The result suggest to leave groundnut oil out of all foods and drugs given to infants and young children, as required for infantile milk formulas.

Animals↗

PubMed2006

Effects of peanut oil load on energy expenditure, body composition, lipid profile, and appetite in lean and overweight adults.

OBJECTIVE: We evaluated the effects of peanut oil intake on appetite, energy expenditure, body composition, and lipid profile in lean and overweight adults. METHODS: In a parallel-arm, long-term feeding trial, lean and overweight participants received a daily peanut oil load in a milk shake equivalent to 30% of their resting energy expenditure for 8 wk. Forty-eight adults (24 lean and 24 overweight, 12 male and 12 female in each group) completed the protocol. Anthropometric indices, appetite, dietary intake, energy expenditure, and plasma lipids were monitored. RESULTS: Energy intake increased significantly in the overweight but not in the lean participants. A statistically significant body weight gain (median 2.35 kg) was also observed among the overweight subjects, although this corresponded to only 43% of the theoretical weight gain. Among overweight subjects, high-density lipoprotein cholesterol increased significantly and low-density lipoprotein cholesterol decreased at week 4, but neither concentration was significantly different from baseline at week 8. Similar, but less marked, changes were observed in lean subjects. Resting energy expenditure was 5% greater (P < 0.01) in the overweight group, but no significant difference was observed in the lean subjects. No marked differences of appetite were observed over time in either group or between overweight and lean participants. CONCLUSION: These data indicate that ingestion of peanut oil elicits a weaker compensatory dietary response among overweight compared with lean individuals. Body weight increased, albeit less than theoretically predicted. The weaker effect of whole nuts on body weight reported in previous studies suggests components other than oil may be responsible.

Adult↗

PubMed2003

Oil quality and sugar content of peanuts (Arachis hypogaea) grown in Argentina: their relationship with climatic variables and seed yield.

The ratio of oleic to linoleic acids (O/L) and the tocopherol content are important features in determining peanut (Arachis hypogaea) seed shelf life. Soluble carbohydrates are known to be important precursors in roasted peanut flavor. The chemical qualities of Argentine grain are different from those of other countries, but no previous studies that associate grain quality and environmental parameters have been performed. Relationships were determined between O/L, tocopherol and sugar contents, and variations in temperature and rainfall during the grain filling period of Florman INTA peanuts. Dry seed yield was used as another explanatory variable. Multiple regression procedure gave mean temperature (positive coefficient) and total precipitation (negative coefficient) as the explanatory variables for variations in O/L. Total precipitation and dry seed yield (both negative coefficients) were found to be predictor variables for tocopherol and sugar contents. Total precipitation was an explanatory variable included in all of the linear regression models obtained in this study.

Arachis↗

PubMed1994

Crystal structure of peanut lectin, a protein with an unusual quaternary structure.

The x-ray crystal structure of the tetrameric T-antigen-binding lectin from peanut, M(r) 110,000, has been determined by using the multiple isomorphous replacement method and refined to an R value of 0.218 for 22,155 reflections within the 10- to 2.95-A resolution range. Each subunit has essentially the same characteristic tertiary fold that is found in other legume lectins. The structure, however, exhibits an unusual quaternary arrangement of subunits. Unlike other well-characterized tetrameric proteins with identical subunits, peanut lectin has neither 222 (D2) nor fourfold (C4) symmetry. A noncrystallographic twofold axis relates two halves of the molecule. The two monomers in each half are related by a local twofold axis. The mutual disposition of the axes is such that they do not lead to a closed point group. Furthermore, the structure of peanut lectin demonstrates that differences in subunit arrangement in legume lectins could be due to factors intrinsic to the protein molecule and, contrary to earlier suggestions, are not necessarily caused by interactions involving covalently linked sugar. The structure provides a useful framework for exploring the structural basis and the functional implications of the variability in the subunit arrangement in legume lectins despite all of them having nearly the same subunit structure, and also for investigating the general problem of "open" quaternary assembly in oligomeric proteins.

Arachis↗

PubMed2004

Structural plasticity of peanut lectin: an X-ray analysis involving variation in pH, ligand binding and crystal structure.

Until recently, it has only been possible to grow crystals of peanut lectin when complexed with sugar ligands. It is now shown that it is possible to grow peanut lectin crystals at acidic pH in the presence of oligopeptides corresponding to a loop in the lectin molecule. Crystals have also been prepared in the presence of these peptides as well as lactose. Low-pH crystal forms of the lectin-lactose complex similar to those obtained at neutral pH have also been grown. Thus, crystals of peanut lectin grown under different environmental conditions, at two pH values with and without sugar bound to the lectin, are now available. They have been used to explore the plasticity and hydration of the molecule. A detailed comparison between different structures shows that the lectin molecule is sturdy and that the effect of changes in pH, ligand binding and environment on it is small. The region involving the curved front beta-sheet and the loops around the second hydrophobic core is comparatively rigid. The back beta-sheet involved in quaternary association, which exhibits considerable variability, is substantially flexible, as is the sugar-binding region. The numbers of invariant water molecules in the hydration shell are small and they are mainly involved in metal coordination or in stabilizing unusual structural features. Small consistent movements occur in the combining site upon sugar binding, although the site is essentially preformed.

Binding Sites↗

PubMed1988

Comparison of peanut agglutinin and S100 stains in the paraffin tissue diagnosis of Langerhans cell histiocytosis.

We compared peanut agglutinin and S100 stains on paraffin embedded material from a variety of sites involved in Langerhans cell histiocytosis (LCH). The two techniques were comparable in terms of ease of performance, time taken and cost. Peanut agglutinin produced dense cell surface and paranuclear staining of the characteristic LCH cells seen in lesions, which was easier to distinguish than the more diffuse cytoplasmic staining produced by the S100 technique. This characteristic staining pattern is more specific than that for the S100 protein which is present in a variety of different cells, including some malignant histiocytes. We recommend that peanut agglutinin be used as a routine diagnostic test for all samples suspected of being LCH.

Histiocytosis, Langerhans-Cell↗

PubMed1982

Binding of disaccharides by peanut agglutinin as studied by ultraviolet difference spectroscopy.

The binding of the disaccharides methyl beta-D-lactoside and 2-acetamido-2-deoxy-3-O-(beta-D-galactopyranosyl)-beta-D-galactopyranose [beta-D-Gal-(l leads to 3)-D-GalNAc] to peanut agglutinin was studied by ultraviolet difference spectroscopy. The magnitude of the difference spectra varied with the concentration of the carbohydrates; association constants and thermodynamic parameters were determined from titration experiments at different temperatures. The enthalpy and entropy changes for binding of methyl beta-D-lactoside were found to be delta H degree = -65 +/- 4 kJ mol-1, delta S degree = -156 +/- 14 J mol-1 K-1. For beta-D-Gal-(1 leads to 3)-D-GalNAc the observed thermodynamic parameters were delta H degree = -78 +/- 5 kJ mol-1,, delta S degree = -177 +/- 16 J mol-1 K-1. For both disaccharides, the enthalpy change upon binding to the lectin is much larger than found for the binding site on peanut agglutinin. The observed parameters are compared with those found for the binding of monosaccharides and oligosaccharides to other lectins and to lysozyme. Molecular models of the minimum energy conformers of beta-D-Gal(1 leads to 3)-D-GalNAc and methyl beta-D-lactoside are used to interpret the interaction of these, and structurally related ligands, with the peanut agglutinin binding site.

Antigens, Tumor-Associated, Carbohydrate↗

PubMed1991

The amino acid sequence of peanut agglutinin.

The amino acid sequence of peanut (Arachis hypogaea) agglutinin was determined from three major fragments obtained by mild acid cleavage at Asp-Pro peptide bonds. The sequence of 236 amino acids has residues identical to those that form the metal-binding site and the hydrophobic pocket in concanavalin A and other lectins, although the overall similarity is only 42%. In the segments of peanut agglutinin that correspond to the four loops that form the carbohydrate-binding site in concanavalin A and favin, several central residues are homologous, while others show changes to smaller side chains, such as Tyr----Gly. The carbohydrate-binding site of peanut agglutinin may therefore have a similar peptide-backbone architecture, but form a considerably more open cleft.

Amino Acid Sequence↗

PubMed1995

Morphologic examination of rabbit nasal mucosa after the nasal administration of insulin peanut oil suspension and a powder dosage form with soybean-derived sterylglucoside.

Soybean-derived sterylglucoside mixture (SG) is a potentially effective absorption enhancer for the nasal absorption of insulin. Insulin is a peanut oil suspension dosage form and in a powder dosage form with SG were administered into the rabbit nasal cavity. After 0.5 or 1 h, nasal mucosa was taken from the nasal cavity and side effects were examined by an optiphoto light microscope. The insulin in the peanut oil suspension produced a histological change in the nasal epithelium mucosae, as well as mucodermal phlogistic cellular infiltration. The peanut oil suspension with SG showed side effects slightly stronger than without SG. SG alone and the insulin powder dosage form with SG produced no signs of inflammation, erosion or squamous metaplasia. The results from this study indicate that SG can be considered safe.

Administration, Intranasal↗

PubMed1999

[Measurement and levels of aflatoxins in small-scale pressed peanut oil prepared in the Diourbel and Kaolack regions of Senegal].

Aflatoxins are mycotoxins produced by some strains of fungus (Aspergillus) which develops in peanuts seeds. Peanuts oil and past are very used up in Senegal, then the aflatoxins poisoning risk are very actual. This study relates to the determination of contamination levels by aflatoxins from peanut oil food prepared by small scale production in areas of Kaolack and Diourbel. High Performance Liquid Chromatography (HPLC) analysis of the different samples showed that 80% of them were contaminated in the areas of Kaolack and Diourbel. Aflatoxin B1, B2, G1 and G2 has been detected with a profile of contamination almost identical in the both areas. Aflatoxin B1 was prevalent and has been found in over 85% of samples. Mean contents of this mycotoxin (the most dangerous toxin) is about 40 ppb, value widely superior to allowable specifications.

Aflatoxin B1↗

PubMedDate not supplied

Peanut allergy: an increasing health risk for children.

Matthew, age 24 months, is brought into the clinic by his frantic mother. She reports Matthew started wheezing and broke out in a blotchy skin rash within 5 minutes of eating a cracker with peanut butter. Matthew has a history of mild, intermittent asthma treated with nebulized albuterol, which the mother administered without improvement in the child's breathing pattern. He also has a history of moderate atopic dermatitis and a prior milk intolerance that he has since outgrown. No other food allergies are noted in his history, and the mother believes this is the first time Matthew has eaten peanut butter. It has been approximately fi hour since he ingested the peanut butter. Matthew's vital signs are temperature 98.6 degrees F, pulse 90, and respirations 60 with audible wheezing and repetitive cough. His blood pressure is 80/60. His face and chest are flushed with urticaria, and some swelling is noted around his mouth.

Child, Preschool↗

PubMed2004

[Hidden food allergens: peanut and gluten--in Polish foodstuffs].

Undeclared allergens in processed products represent a major health problem for sensitized persons. Peanut flour and gluten are known as potent food allergens. The study was designed to evaluate with enzymeimmunoassay (ELISA) test kits the presence of gluten and peanut in Polish products. Hidden peanut contamination was detected in 4 of 34 (11.8%) processed foods (corn crisps, wafers, cereal bar and halva). 5 of 37 (13.5%) foodstuffs (cornflakes, corn crisps, bouillon cube, vegetable soup for infants, curry powder) contained undeclared gluten. The nutritional management of sensitized persons with food allergy requires new labeling regulations.

Allergens↗

PubMed2005

[Preparation of 5-fluorouracil-peanut agglutinin conjugate and determination of the ratio of drug to conjugate].

5-fluorouracil was combined with peanut agglutinin by a water-soluble carbodiimide to prepare the tumor target conjugate of 5-fluorouracil-peanut agglutinin and the ratio of drug to conjugate was determined by the modified trinitrobenzenesulfonic acid method (TNBS). The ratio of drug to conjugate was 76.33%. The result showed that 5-fluorouracil could link to the peanut agglutinin by EDC/NHS crosslinking with high drug ratio.

Antineoplastic Agents↗

PubMed1983

Purification of peanut agglutinin by affinity chromatography on asialoglycophorin from human erythrocytes.

A simple and efficient method of purification of peanut agglutinin is described. This method involves affinity chromatography on human asialoglycophorin linked to Affi-Gel. One milliliter of the packed adsorbent contained 1.7 mg of covalently linked asialoglycophorin and bound about 6 mg of the peanut agglutinin. From 250 g of row peanuts 510 mg of the electrophoretically homogeneous lectin with high agglutinating activity was obtained.

Asialoglycoproteins↗