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At least 19 recordsLinked to original sources

PubMed1995

Effect of cooking on proteinase inhibitors of Dolichos lablab bean (Dolichos lablab perpureus L.).

Proteinase inhibitory activity in ten different varieties of Dolichos lablab perpureus. L. was determined. All the varieties tested exhibited appreciable level of proteinase inhibitory activity (PIA). The trypsin inhibitory activity (TIA) (Mean: 20170 TIU/g) was relatively higher than the chymotrypsin inhibitory activity (CIA) (Mean: 15380 CIU/g). Effect of temperature and cooking on PIA was studied. The nature of cooking medium and duration of cooking had profound effect on the PIA. The dry fried seeds lost their PIA very rapidly (91% in 20 min). Seeds cooked in slightly alkaline medium lost their PIA quickly (89% in 30 min) compared to those cooked in acidic (80% in 30 min) and neutral pH (83% in 30 min). The PIA in green pods was also determined and they had only one third of the PIA (8200 TIU/g and 8125 CIU/g) found in the dry seeds.

Fabaceae↗

PubMed1975

Interaction between Dolichos biflorus lectin and chick embryonic fibroblasts at different stages of development.

The interaction between chick embryo fibroblasts and A1-specific blood group Dolichos biflorus lectin has been studied at various stages of embryo development. The site number ((0.26 plus or minus 0.03)-10-6 sites/cell) remains the same during development whereas the affinity constant apparently decreases from 8-day cells onwards. The effects of cell number, temperature and time course on the Dolichos binding to fibroblasts were not age dependent. Competitive binding experiments revealed that Dolichos receptor sites were distinct from binding sites fo Robina pseudoacacia lectin and concanavalin A, but partially related to binding sites of Ricinus lectin. Thymidine incorporation by fibroblasts in the presence of Dolichos lectin was age dependent. It was inhibited in 6-day cells and weakly stimulated in 16-day cells, but not modified in 12-day cells. Dolichos lectin effects on embryo fibroblasts were very specific because both binding to cells and effect on thymidine incorporation were blocked by N-acetylgalactosamine, the determinant of Dolichos lectin, as well as by Dolichos antiserum.

Animals↗

PubMed1975

Cell growth and thymidine incorporation changes induced by Dolichos lectin in embryo fibroblasts at various stages of differentiation.

We report here the effect of Dolichos lectin on chick embryo fibroblasts from embryos between 6th and 16th day of development. There is evidence that Dolichos lectin decreases cell number and proportion of cells incorporating tritium labelled thymidine in case of chick embryo fibroblasts of 6th, 8th and 10th day of development. Dolichos lectin stimulated the proliferation of 16-day old embryo cells. No effect was noticed on 12-day embryo cells at different concentrations of Dolichos lectin used. This lectin is specifically inhibited by N-acetyl-D-galactosamine and anti-Dolichos lectin serum. The difference in response by cells during different stages of embryonic development could perhaps be explained as some regulatory changes occurring on the cell surface.

Acetylgalactosamine↗

PubMed1997

Metabolism of dolichol, dolichoic acid and nordolichoic acid in cultured cells.

The uptake and metabolism of [1-(14)C]-labelled dolichol, dolichoic acid and nordolichoic acid were investigated in MDCK and HepG2 cells. Each of the three isoprenoids, bound to human serum albumin, was taken up effectively. None of the compounds was broken down in HepG2 cells, although these converted dolichol into fatty acid esters. In MDCK cells dolichoic acid gave rise to the formation of [14C]CO2 and radiolabelled formic acid, indicating that dolichoic acid can be broken down by alpha-oxidation. Dolichoic acid was also converted to a mixture of polar compounds, possibly polyols. MDCK cells generated radiolabelled CO2 from nordolichoic acid, presumably through beta-oxidation, although we could not find any labelled propionic acid. No oxidative breakdown of dolichol was found, apparently due to the lack of or very low conversion to dolichoic acid.

Animals↗

PubMed1993

Heterogeneous Dolichos biflorus lectin binding to a subset of rat alveolar macrophages in normal and fibrotic lung tissue.

The distribution of Dolichos biflorus lectin in the rat lung and during fibrosis after irradiation was investigated by lectin histochemical and electron microscopical techniques and double immunofluorescence labelling with the monoclonal antibodies RM-1 and ED-1. The results indicate a selective reaction of Dolichos biflorus lectin with a subpopulation of alveolar macrophages. No binding of the lectin was detectable in ED-1-positive macrophages but strong staining occurred in a part of the RM-1-positive cell population. In fibrotic lung specimens an increased number of Dolichos biflorus lectin-positive macrophages was found in which focally ED-1 reactive and RM-1 negative cells appeared. The finding of changing lectin binding pattern in a radiation-induced lung model emphasizes the suitability of the Dolichos biflorus lectin as a marker of macrophage activation or functional specialization.

Animals↗

PubMed1983

Immunochemical studies on the combining sites of Forssman hapten reactive hemagglutinins from Dolichos biflorus, Helix pomatia, and Wistaria floribunda.

The lectin of Dolichos biflorus, a hemagglutinin previously considered to be blood group A specific, is now found to react much more strongly with the terminal disaccharide unit [alpha DGalNAc(1 leads to 3) beta DGalNAc] of the Forssman antigenic determinant. In contrast, the relative reactions of the lectins of Helix pomatia (which also agglutinates A erythrocytes) and Wistaria floribunda (which agglutinates A, B, and O erythrocytes) with the Forssman pentasaccharide were substantially weaker than that of Dolichos biflorus. The combining site of the lectin of Helix pomatia has a broader affinity for terminal 2-acetamido-2-deoxy-alpha-D-galactopyranose (alpha DGalNAc) residues than does that of Dolichos biflorus. The reactions of the lectin with terminal alpha DGalNAc units are strongly dependent on the nature of the aglycon and remain ill defined. The lectin may also react with appropriately presented terminal 2-acetamido-2-deoxy-beta-D-glucopyranose units. The broad affinity of the lectin of Wistaria floribunda which reacts both with a range of blood group specific glycoproteins (A, B, H, Lea, and Leb) and with non blood group glycoproteins [Sugii, S., & Kabat, E.A. (1980) Biochemistry 19, 1192-1199] appears best assigned to a combining site that favors pauci- or multivalent cooperative effects of clustered terminal beta-D-galactopyranose units. An attempt is made to rationalize certain of the inhibition data in terms of topographical features at the surfaces of the carbohydrate structures which are considered compatible for binding within essentially hydrophobic combining sites.

ABO Blood-Group System↗

PubMed1976

Immunochemical studies on blood groups LXII. Fractionation of hog and human A, H, and AH blood group active substance on insoluble immunoadsorbents of Dolichos and Lotus lectins.

The purified lectins from Lotus tetragonolobus and Dolichos biflorus were coupled to Sepharose 2B to make insoluble adsorbents for purification and fractionation of blood group A and H active glycoproteins. With both adsorbents, hog gastric mucin A + H blood substance (HGM), purified by phenol-ethanol precipitation, yielded fractions showing only A, only H, or AH activities. The AH fraction was obtained when the adsorbent column was overloaded with HGM and its A and H specificities seem to be carried on the same molecules since they were not separable by chromatography on either column. However A and H specificities of blood group substance from the stomach of a presumably heterozygous individual hog were both on the same molecules as they too could not be fractionated on either column. Analytical properties of the isolated fractions were generally similar to those of the unfractionated material, the purfied A substances had a higher galactosamine/fucose ratio than did the H substances. Although the original A + H showed very little specific optical rotation, the separated A and H substances rotated positively and negatively, respectively. The lectin-Sepharose adsorbents have also proven useful in isolating A or H substances directly from the crude commercial hog gastric mucin. Blood group A2 substance from a human ovarian cyst yielded two fractions on the Lotus-Sepharose column; the effluent did not interact with the Lotus lectin but precipitated the Ulex and Dolichos lectins and anti-A, and appears to contain type 1 H determinants. The other fraction reacted with Lotus and Ulex lectin as well as with Dolichos and anti-A.

ABO Blood-Group System↗

PubMed1999

Purification and characterization of Dolichos lablab lectin.

The mannose/glucose-binding Dolichos lablab lectin (designated DLL) has been purified from seeds of Dolichos lablab (hyacinth bean) to electrophoretic homogeneity by affinity chromatography on an ovalbumin-Sepharose 4B column. The purified lectin gave a single symmetric protein peak with an apparent molecular mass of 67 kDa on gel filtration chromatography, and five bands ranging from 10 kDa to 22 kDa upon SDS-PAGE. N-Terminal sequence analysis of these bands revealed subunit heterogeneity due to posttranslational proteolytic truncation at different sites mostly at the carboxyl terminus. The carbohydrate binding properties of the purified lectin were investigated by three different approaches: hemagglutination inhibition assay, quantitative precipitation inhibition assay, and ELISA. On the basis of these studies, it is concluded that the Dolichos lablab lectin has neither an extended carbohydrate combining site, nor a hydrophobic binding site adjacent to it. The carbohydrate combining site of DLL appears to most effectively accommodate a nonreducing terminal alpha-d-mannosyl unit, and to be complementary to the C-3, C-4, and C-6 equatorial hydroxyl groups of alpha-d-mannopyranosyl and alpha-d-glucopyranosyl residues. DLL strongly precipitates murine IgM but not IgG, and the recent finding that this lectin interacts specifically with NIH 3T3 fibroblasts transfected with the Flt3 tyrosine kinase receptor and preserves human cord blood stem cells and progenitors in a quiescent state for prolonged periods in culture, make this lectin a valuable tool in biomedical research.

Carbohydrate Metabolism↗

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↗

PubMed2000

Symptomatic unilateral dolicho-ectasia of the intracranial arteries in a child.

Dolicho-ectasia of the left posterior cerebral artery and internal carotid artery in a 5-year-old boy is reported. There was compression of the brainstem, the mammillary bodies and the optic tract. The value of MR angiography in the diagnosis of this vascular anomaly is demonstrated. Dolicho-ectasia of more than one cerebral artery in a child is extremely rare.

Arteries↗

PubMed1993

Characterization of the in vitro conversion of dolichol to dolichoate in bovine thyroid.

The enzymic conversion of dolichol into dolichoic acid has been studied in bovine thyroid subcellular fractions using [1-3H]dolichol as a substrate. The presence of conversion activity could be demonstrated in both the mitochondrial- and supernatant fractions. Investigation of cofactor requirements revealed that NAD+ was essential for reaching optimal activity. From kinetic studies Km-values of 3.5-4 microM and 0.29 mM could be calculated for, respectively, dolichol and NAD+ using the mitochondrial fraction as an enzyme source. No inhibitory effects from ethanol or pyrazole were detected suggesting that alcohol dehydrogenase is not involved in the dolichol-->dolichoate conversion as observed in a bovine thyroid mitochondrial fraction. From inhibitor studies the conversion system behaves distinctly differently from the NADP(+)-depending microsomal oxidoreductase as well as from catalase. The conversion activity in the supernatant on the other hand must be ascribed, at least partially, to a side activity of alcohol dehydrogenase.

Alcohol Dehydrogenase↗

PubMed1975

Circular dichroism and conformational transition of Dolichos biflorus and Robinia pseudoacacia lectins.

The conformation of the lectins from Dolichos biflorus and Robinia pseudoacacia was studied by means of circular dichroism (CD). It was found that N-acetyl-D-galactosamine induced significant changes in the near-ultraviolet CD spectrum of Dolichos lectin but was ineffective with the lectin from Robinia. Tyrosine and tryptophan chromophores were chiefly involved in this saccharide-lectin interaction. The far-ultraviolet CD spectra indicated that both lectins have a significant content of the pleated sheet conformation, but not much, if any, alpha-helix. The predominant conformation in these lectins is the aperiodic bend structure which is stabilized chiefly by hydrophobic interactions. This was ascertained by the effect of sodium dodecylsulfate on these proteins.

Acetylgalactosamine↗

PubMed1990

Ethylnitrosourea-induced mutations in vivo involving the Dolichos biflorus agglutinin receptor in mouse intestinal epithelium.

A mutagenesis assay system is introduced based on the induction of mutations in somatic cells of mouse small intestine using ethylnitrosourea (ENU). F1 mice heterozygous for the Dolichos biflorus agglutinin (DBA) locus (Dlb-1a/Dlb-1b) encoding the DBA cell surface receptor, were treated in utero on either day 7, day 9 or day 11 post coitum. Mutant intestinal cell populations of adult mice were visualised in whole-mount preparations by the absence of histochemical staining using peroxidase-labelled Dolichos biflorus agglutinin. Loss of staining is attributed to mutagenesis of the Dlb-1b allele in the heterozygote. This system allows one to evaluate mammalian mutagenesis in vivo at a single locus. Mutant cell populations appeared as discrete groups of 'striped' villi, each stripe comprising cells derived from unstained crypt stem cells (cf. Schmidt et al., 1985a). A spontaneous mutation level was noted in untreated controls which was found to differ significantly from that recorded in mice treated with the mutagen (P less than 0.01). The mutation scores were highly consistent among mice and a small number of animals (i.e., 16) were sufficient to detect mutagenic effects of ENU. Thus, the advantages which accrue from the assay are (1) the ability to detect small clones of mutant cell populations in the intestine (i.e., cells derived from a single mutated crypt); (2) a small number of tested mice are required to generate a conclusive result, especially when compared to the mammalian spot test (Fahrig, 1978).

Analysis of Variance↗

PubMed1978

Immunochemical studies on blood groups LXVI. Competitive binding assays of A1 and A2 blood group substances with insolubilized anti-A serum and insolubilized A agglutinin from Dolichos biflorus.

Competitive binding assays using 3H-labeled blood group A substance and insolubilized Dolichos biflorus lectin or human anti-A were carried out, measuring competition by blood group A1 and A2 glycoproteins, and by unabsorbed anti-A sera, and with these sera absorbed with the A1 and A2 glycoproteins. With Dolichos lectin specific for (formula: see text) A1 substances had about 11 times as many determinants as did A2 substances, but the slopes of the lines in the competitive binding assays were the same. With insolubilized anti-A, A2 substances gave lines of lower slopes. Although individual A1 populations varied in the amounts giving 50% inhibition in the assays, as did A2 substances, the slopes of the lines for the A1 substances were the same and always higher than the slopes of the lines for the A2 substances. Competitive binding assays with unabsorbed anti-A sera and with these sera absorbed with insoluble polyleucyl A1 and A2 substances showed that partial absorption of polyleucyl A1 substances left antibodies of lower slope in the supernate, whereas absorption with polyleucyl A2 substance left antibodies (anti-A1) having the same or an even higher slope than the unabsorbed sera. The findings indicate that human A1 and A2 glycoproteins differ in their determinants, and that A2 specificity is determined by the type 2 chain in which the A trisaccharide (formula: see text) is linked beta 1 leads to 4 to DGlcNAc, whereas the A1 specificity is determined by the type 1 chain in which this trisaccharide is linked beta 1 leads to 3 to DGlcNAc; most of the determinants in the glycoproteins have a second LFuc linked alpha 1 leads to 3 and alpha 1 leads to 4 to the DGlcNAc of the type 2 and type 1 chains, respectively.

ABO Blood-Group System↗

PubMed1984

Development and Distribution of a Lectin from the Stems and Leaves of Dolichos biflorus.

The stems and leaves of the Dolichos biflorus plant contain a lectin that cross-reacts with antiserum against the seed lectin. This cross-reactive material (CRM) was followed during early seedling growth, stem elongation, and seed development using a specific radioimmunoassay.No CRM was detected in developing seeds, but very low levels were found in dormant and imbibed seeds. As germination proceeds, the CRM accumulates at the apex of both etiolated and green seedlings in the epicotyl and leaves. Lower amounts of CRM are found in the cotyledons and hypocotyl, but no CRM was detected in the roots.The amount of CRM in the first and second stem internodes increases during elongation and gradually declines after the completion of elongation. Approximately 80% of the CRM in the stems of 19-day-old Dolichos biflorus plants is associated with the elongating tissues. These results are discussed with respect to the possible roles of lectins in plants.

Journal Article↗

PubMed1976

Cad(super Sda) in a British family with eastern connections: a note on the specificity of the Dolichos biflorus lectin.

Cad, Sd(a++) or Super Sda is a rare, inherited, dominant blood group character which is of much interest, not only with regard to problems in pretransfusion tests (erythrocyte polyagglutination) but also in the field of lectin specificity. We have studied this blood group character in a British family with Eastern connections and present a brief account of its serological and clinical importance. Most persons are Sd(a+) but there is a wide distribution of antigen strength, ranging from ordinary Sd(a+) to Cad. Most persons also have weak anti-Sda in their serum; this is ordinarily of no clinical importance, but could cause problems if Cad bloods are transfused. The chief structural determinant of Cad specificity is N-acetyl-D-galactosamine in alpha-linked position, yet it is clearly distinguishable by use of appropriate lectins from other blood group antigens, A and Tn, which also have this acetyl-hexosamine as their chief structural determinant. A method for the rapid identification of Cad, applicable to all ABO groups, is described. The lectin of Dolichos biflorus, which is specific for N-acetyl-D-galactosamine in alpha-linked position, reacts strongly with A(A1), Tn and Cad cells, its action on Cad cells being much the strongest. Absorption-elution studies show that one and the same lectin reacts with both A1 and Tn cells. Absorption with Cad cells abolishes activity for A1, Tn and Cad cells; whereas absorption with A1 or Tn cells leaves activity for Cad. This does not necessarily indicate that anti-Cad is a separate component since the same result can be obtained by simply diluting the Dolichos reagent. However, eluates from Cad cells react only with Cad cells, whereas eluates from A1 or Tn cells react with A1, Tn and Cad cells.

ABO Blood-Group System↗

PubMed1988

Hemagglutinating activity of Dolichos lablab seed protein.

The hemagglutinating activity of a crude extract and partially purified protein fractions from seeds of Dolichos lablab grown in the state of Bahia, Brazil, has been examined. The crude extract agglutinates rabbit erythrocytes non-specifically with respect to blood groups. The hemagglutination of rabbit erythrocytes induced by the crude extract of D. lablab was inhibited most effectively by N-acetyl-D-glucosamine (3 mM) and alpha-methyl-D-mannoside (3 mM) followed by D-glucosamine (6 mM), D-mannose (6 mM) and D-glucose (12 mM). The spectrum of sugar inhibition of the hemagglutinating activity of the Brazilian seeds combines the characteristics of seeds coming from Turkey and India as indicated by the preferential inhibitory effect exerted by N-acetyl-D-glucosamine and the inhibition by D-mannose and D-glucose. These data suggest that the Brazilian seeds may belong to a different variety of Dolichos lablab.

Acetylglucosamine↗

PubMed1985

An allelic difference determines reciprocal patterns of expression of binding sites for Dolichos biflorus lectin in inbred strains of mice.

We used staining of tissue sections by lectin conjugates to screen inbred strains of mice for polymorphisms which could be used as histological markers of chimaerism. We found one polymorphism, which involves reciprocal patterns of expression of binding sites for the N-acetyl-galactosamine-binding lectins from Dolichos biflorus (DBA), Helix pomatia (HPA) and Wisteria floribunda (WFA) on intestinal epithelium and vascular endothelium. The polymorphism is due to alleles at a single locus, designated D1b-1 (for Dolichos lectin binding). Of 29 inbred strains examined, 3 are D1b-1a (type strain RIII-ro; gut epithelium-ve, vascular endothelium + ve), and 26 are D1b-1b (type strain C57BL/6J; gut epithelium + ve, vascular endothelium-ve). In RIII-ro and C57BL/6J embryos, the polymorphic difference is not clearly present until day 11 of gestation. Before then, embryos of both strains express binding sites on gut epithelium and on endothelium. The temporal and tissue-specific patterns of expression of lectin-binding sites may result from differences in expression of an N-acetyl galactosaminosyl transferase. If so, elucidation of the genetic basis of the polymorphism might provide an insight into the mechanisms of developmental regulation of glycosyltransferase activity.

Alleles↗