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PubMed1979

The nutritional toxicity of Phaseolus vulgaris lectins.

In rats fed on beans (Phaseolus vulgaris) the poorly digestible lectins were shown to react with intestinal cells in vivo and to cause a disruption of many of the brush borders of duodenal and jejunal enterocytes. Although depressed to a certain extent, absorption still occurred, probably through the non-disrupted cells of the small intestine. In addition, abnormal absorption of potentially harmful substances, lectin-related or of bacterial origin, could also occur, possibly as a direct effect of the disruption caused by the lectins on the enterocytes. It is suggested that toxicity was the result of ensuing systemic effects, such as for example the observed high N excretion possibly through increased tissue catabolism.

Animals↗

PubMed1979

Effect of gamma irradiation on nutritional value of dry field beans (Phaseolus vulgaris) for chicks.

The effect of gamma irradiation (60Co) of different varieties and breeding lines of dry field beans (Phaseolus vulgaris) on chick growth was determined using a chick growth assay in which the diet contained approximately 50% beans. Total protein (N X 6.25) in beans was not changed appreciably by irradiation (21 Mrad) but protein solubility in water was decreased. Irradiation increased in vitro enzymatic digestibility of bean protein by pepsin and by a mixture of trypsin, chymotrypsin and peptidase. In the bioassay the diet was formulated to derive half of the total protein (22.6%) from beans. Autoclaved Pinto and Pink beans gave significantly better growth than Red Mexican and White Pea beans. The differences between Red Mexican and White Pea beans were not significant except for Red Mexican breeding line number RS-59. The nutritional value of all varieties of beans, based on chick growth, was significantly improved by gamma irradiation. The irradiation treatment of beans tended to increase nitrogen retention by chicks and decrease uric acid nitrogen excretion in relation to nitrogen intake.

Animal Feed↗

PubMed1975

Purification and characterization of proteinase inhibitors from adzuki beans (Phaseolus angularis).

Two proteinase inhibitors, designated as inhibitors I and II, were purified from adzuki beans (Phaseolus angularis) by chromatographies on DEAE- and CM-cellulose, and gel filtration on a Sephadex G-100 column. Each inhibitor shows unique inhibitory activities. Inhibitor I was a powerful inhibitor of trypsin [EC 3.4.21.4], but essentially not of chymotrypsin ]EC 3.4.21.1]. On the other hand, inhibitor II inhibited chymotrypsin more strongly than trypsin. The molecular weights estimated from the enzyme inhibition were 3,750 and 9,700 for inhibitors I and II, respectively, assuming that the inhibitions were stoichiometric and in 1 : 1 molar ratio. The amino acid compositions of both inhibitors closely resemble those of low molecular weight inhibitors of other leguminous seeds: they contain large amounts of half-cystine, aspartic acid and serine, and little or no hydrophobic and aromatic amino acids. Inhibitor I lacks both tyrosine and tryptophan residues. The molecular weights were calculated to be 7,894 and 8,620 for inhibitors I and II, respectively. The reliability of these molecular weights was confirmed by the sedimentation equilibrium and 6 M guanidine gel filtration methods. On comparison with the values obtained from enzyme inhibition, it was concluded that inhibitor I and two trypsin inhibitory sites on the molecule, whereas inhibitor II had one chymotrypsin and one trypsin inhibitory sites on the molecule.

Amino Acids↗

PubMed1976

3-Dehydroquinate synthase in germinating Phaseolus mungo seedlings.

Dehydroquinate synthase, an enzyme catalyzing the conversion of 3-deoxy-D-arabino-heptulosonate 7-phosphate (DAHP) to 3-dehydroquinate, was detected in cell-free extracts of etiolated Phaseolus mungo seedlings. The reaction product, 3-dehydroquinate, formed from [1-14C]DAHP was identified by paper-radiochromatography. The enzyme required NAD+ and Co2+ for activity.

Cations, Divalent↗

PubMed2026

Genomic Regions Associated with Resistance to Soybean Cyst Nematode (Heterodera glycines Ichinohe) Population HG Type 1.2.5.7 in Dry Beans (Phaseolus vulgaris L.).

North Dakota, the largest dry bean (Phaseolus vulgaris L.) producing state in the U.S., faces an emerging production threat caused by the soybean cyst nematode (SCN; Heterodera glycines Ichinohe, 1952). Host resistance is an effective management strategy, yet resistance to the virulent SCN population HG type 1.2.5.7 has not been genetically characterized in dry beans. In this study, 170 dry bean genotypes (113 breeding lines/cultivars and 57 germplasm accessions) were evaluated for response to HG type 1.2.5.7 under controlled conditions using female index (FI) as the resistance phenotype. FI values ranged from 4.1% to 78.1%, with one genotype (PI 313733) classified as resistant, 35 moderately resistant, 104 moderately susceptible, and 30 susceptible. Genome-wide association analysis using 2,044 single-nucleotide polymorphism (SNP) markers from the 3.8K Bean Panel chip and the BLINK model identified four significant marker-trait associations on chromosomes Pv02, Pv05, Pv07, and Pv11. Linkage disequilibrium-defined candidate intervals spanned 108 kb (Pv02), 1.50 Mb (Pv05), 798 kb (Pv07), and 1.45 Mb (Pv11), collectively containing 126 annotated genes: 20 on Pv02, 39 on Pv05, 35 on Pv07, and 32 on Pv11. The intervals contained putative genes annotated for signaling and transcriptional regulation, cell wall and carbohydrate metabolism, transport, and secondary metabolism. Together, these findings indicate that the response to HG type 1.2.5.7 in dry bean is quantitative and associated with multiple genomic regions. The identified intervals provide candidate targets for independent validation, fine mapping, functional analysis, and future marker development to support breeding for SCN resistance.

Disease Resistance↗

PubMed1975

The amino-acid sequence of leghemoglobin component a from Phaseolus vulgaris (kidney bean).

1. Leghemoglobin component a from Phaseolus vulgaris (kidney bean) was digested with trypsin; 15 tryptic peptides and free lysine were purified and the amino acid sequences of the peptides determined. 2. The internal order of the tryptic peptides was determined by the bridge peptides obtained from the thermolytic digest and the dilute acid hydrolyzate of kidney bean leghemoglobin a; 12 thermolytic peptides and two acid hydrolysis peptides were purified and the sequences were partially or completely determined. 3. The complete amino acid sequence of kidney bean leghemoglobin a is compared to that of leghemoglobin a from soybean (Glycine max) and to some animal globins. As regards sequence, the kidney bean globin has 79% identity with the soybean globin and 21% identity with human hemoglobin gamma-chain. Seven of the 14 amino acid residues common to most globins are found in the kidney bean globin. Trp-15 and Tyr-145 are evolutionarily conserved in this globin, which confirms the concept of a common origin of animal and plant globins.

Amino Acid Sequence↗

PubMed1977

alpha-Mannosidase from Phaseolus vulgaris. Composition and structural properties.

Both alpha-mannosidases I and II from Phaseolus vulgaris have molecular weights about 210000-220000 and contain approximately 2 mol zinc/mol protein. alpha-Mannosidase I seems to consist of more glutamic acid than alpha-mannosidase II, while the latter is richer in serine. They are glycoproteins: alpha-mannosidase I contains 8.3% carbohydrate by weight while alpha-mannosidase II contains 16.5%. This enzyme form shows a greater thermal stability than alpha-mannosidase I. The structure of alpha-mannosidase has been investigated by equilibrium sedimentation analysis in guanidine hydrochloride, electrophoresis in dodecylsulphate, and alkaline electrophoresis after exposure to high pH. The protein appears to be composed of two non-covalently bound subunits of molecular weights about 110000. Electron micrographs revealed images of molecules that consisted of two rod-shaped monomers of roughly square cross-sections 4.2 X 4.2 nm. Each rod was about 7.4 nm long. The monomers seemed parallell along the long axis.

Amino Acids↗

PubMed1978

Isolation and chemical characterization of a highly purified phytomitogen from Phaseolus coccineus seeds.

An effective lymphocyte mitogen with a low erythroagglutinating ability was isolated from the seeds of Phaseolus coccineus L. by ammonium sulphate precipitation and repeated ion-exchange chromatography on modified Sephadex. The mitogen stimulated lymphocytes at concentrations as low as 0.25 microgram/ml, the optimum concentration being in the range of 2.5-5.0 microgram/ml. This stimulating effect was completely inhibited by 5 mg/ml methyl alpha-D-mannopyranoside. Column gel filtration, disc electrophoresis on polyaceylamide gel in an alkaline medium and in the presence of sodium dodecylsulphate and the finding of a single N-terminal amino acid (alanine) showed the phytomitogen to be homogenous. Disc electrophoresis in an acid medium revealed the presence of two or three bands which are assumed to be due to aggregates of the mitogen. The minimum molecular weight, as derived from sodium dodecylsulphate electrophoresis on polyacrylamide, was 35000. The mitogen is a glycoprotein containing 10% neutral sugars and 1.3% amino sugars (glucosamine). The amino acid composition of the isolated phytomitogen is presented.

Amino Acids↗

PubMed2026

Isolation of rhizobia from Ontario soils that are effective at fixing nitrogen with common bean (Phaseolus vulgaris).

UNLABELLED: Common bean (Phaseolus vulgaris) is an important crop in Canada and globally. Like other legumes, common bean establishes symbiotic interactions with nitrogen-fixing bacteria called rhizobia. However, nitrogen fixation by rhizobia in association with common bean is often suboptimal, constraining its productivity and necessitating the application of nitrogen fertilizer. To support the development of high-performing, locally adapted rhizobial inoculants for Ontario common bean growers, we isolated 216 common bean-nodulating rhizobia from southern Ontario soils using a nodule trapping approach with four common bean cultivars. Whole genome sequencing followed by phylogenomic analyses of all rhizobial isolates revealed substantial diversity, assigning them to 11 Rhizobium species, including two novel species. Nearly all isolates belong to the symbiovar phaseoli, spanning the nodC γ-a, γ-b, and α alleles, with four isolates belonging to the symbiovar gallica. Soil origin had a significant impact on the species-level community composition recovered during the nodule trapping experiments. In contrast, host trapping cultivar had only a minor influence on the recovered Rhizobium population. Greenhouse assays demonstrated that one of the novel Rhizobium species exhibited the highest average symbiotic effectiveness, although high-quality isolates were found across multiple species. Together, these results revealed a diverse and genomically variable Rhizobium community capable of forming effective symbioses with common bean in southern Ontario soils. Importantly, our genome-sequenced Rhizobium collection will serve as a valuable resource for identifying competitive and high-quality strains for the development of inoculants tailored to Ontario common bean production. IMPORTANCE: Common bean is a globally important food crop, yet its productivity is often limited by suboptimal nitrogen fixation, forcing growers to rely on synthetic fertilizers. Consequently, identifying high‑performing, locally adapted inoculant strains is essential for reducing dependence on synthetic nitrogen fertilizers and improving the sustainability of temperate agroecosystems. Our study provides a genome‑sequenced collection of common bean-nodulating Rhizobium from southern Ontario, revealing substantial species and genomic diversity across sampling locations. Greenhouse studies allowed us to identify multiple isolates that consistently fix nitrogen with, and enhance the growth of, common bean plants. Our findings highlight strong biogeographical structuring of the effective and competitive subpopulations of rhizobial communities and demonstrate that Ontario soils already harbor strains with high symbiotic potential. In addition, our Rhizobium collection represents a foundational resource to support future inoculant development and enables future work on the ecology, evolution, and applied optimization of legume-rhizobium symbioses.

Nanopore↗

PubMed1978

Nodule infection by bean yellow mosaic virus in Phaseolus vulgaris.

Infection of root nodules of beans, Phaseolus vulgaris L., by bean yellow mosaic virus (BYMV) and the effect of the disease on the specific activity of the nodule are reported. Infectivity and serological microprecipitin assays with two sources of BYMV antiserum demonstrated that nodules from bean plants whose leaves had been inoculated with BYMV contain BYMV antigen. The disease reduced the fresh weights of tops, roots, and root nodules and induced premature nodule decay and/or nodule drop. The disease also reduced leghemoglobin content, on a plant weight basis, and N2 fixation rate, on an individual plant basis, as measured by the acetylene reduction assay. The increased leghemoglobin content per gram-nodule in BYMV-infected nodules relative to healthy nodules might be associated with multiplication of the virus in the nodule and/or unknown cellular effects derived from the BYMV-Rhizobium interaction.

Antigens, Viral↗

PubMed1975

An ultrastructural study of acid phosphatase localization in Phaseolus vulgaris xylem by the use of an azo-dye method.

The localization of acid phosphatase during xylem development has been examined in the bean, Phaseolus vulgaris. The azo dye, the final reaction product, is initially prominent in the dictyosomes, vesicles apparently participating in secondary wall formation, and in the middle lamella of the young vessel element. Final reaction particles are also present in mitochondria, chloroplasts, and certain vacuoles and are sparsely scattered in the cytoplasm. At a later stage of vessel differentiation, the azo dye is concentrated in the disintegrating cytoplasm and along the fibrils of the partially hydrolysed primary wall and middle lamella. In the mature vessel element, the azo dye is still present along the disintegrated primary wall at the side of the vessel and covers the secondary wall. In the parenchyma cell adjacent to the vessel element, acid phosphatase localization is found in the dictyosomes, endoplasmic reticulum, mitochondria, small vacuoles, and the middle lamella. The controls from all stages of vessel element development were free of azo dye particles. The concentration of acid phosphatase along the secondary walls of the mature vessels and in the middle lamella between other cells indicates that this enzyme has other functions besides autolysis of the cytoplasm and primary cell wall. Acid phosphatase may participate in the formation of the secondary wall and may also have a role in the secretion and transport of sugars.

Acid Phosphatase↗

PubMed1979

On the receptors of human red cells reacting with Phaseolus coccineus L. lectin.

In order to elucidate receptors of proteolytic enzyme-treated red cells which react with Phaseolus coccineus L. lectin, the receptors prepared by affinity chromatography were serologically investigated. P. coccineus lectin had high agglutinin activity for bromelin-, papain- and pronase-treated red cells but that for the cells treated with ficin and trypsin was relatively low. Analyses of chemical composition revealed that sialic acid of the receptors from normal red cells was considerably much as compared with that from the treated cells. On the contrary, the enzyme treatment did not affect particularly carbohydrate composition of the receptors. Disc electrophoresis showed that the patterns of receptors from red cells treated with bromelin or papain were different from those from the other cells. On two-dimensional immunoelectrophoresis, the receptor of trypsin-treated cells gave five precipitation lines against anti-stroma and that of papain-treated cells three lines, but any other receptors showed no line. These findings indicate that there are plural receptors for P. coccineus lectin in red cells treated with each of proteolytic enzymes and that the receptors from respective red cells have electrophoretically and serologically different property.

Chromatography, Affinity↗

PubMed1977

The isolation and characterization of a lethal protein from Kintoki beans (Phaseolus vulgaris).

A lethal protein with hemagglutinating activity but without trypsin inhibitory activity was isolated from beans of Phaseolus vulgaris, cultiva, and Kintoki and proved homogeneous by ultracentrifugation, disc polyacrylamide gel electrophoresis, sodium dodesyl sulfate polyacrylamide gel electrophoresis and isoelectric focusing. The molecular weight was estimated to be 104, 000 by ultracentrifugal analysis and gel filtration on Sephadex G-200. The molecule dissociates into three identical subunits in the presence of 8 M urea or 0.1% sodium dodesyl sulfate. The amino acid composition was characterized by the high content of aspartic acid and the complete absence of methionine and cystine. The carbohydrate content was 8.1%; 5.0% mannose and 3.1% glucosamine. The addition of the lethal protein to a basal diet (0.4%) resulted in the intensive depression of the growth and finally in the death of rats. The intraperitoneal injection of 250 microgram per g body weight of mouse brought about an acute toxicity which caused death of all the injected mice.

Amino Acids↗

PubMed1978

The isolation and characterization of a trypsin inhibitor from Kintoki bean (Phaseolus vulgaris).

A trypsin inhibitor was isolated from beans of Phaseolus vulgaris, cultivar. Kintoki, and the specific activity increased 200 times as high as that of the crude extract. It was homogeneous on several electrophoreses and the molecular weight was about 13,000. The amino acid composition was characterized by high ratios of cystine, aspartic acid, and serine. It inhibited trypsin in a molar ratio of 1 : 1 and alpha-chymotrypsin in a molar ratio of 2 : 1. It, however, inhibited neither pepsin nor pronase. It was relatively stable to heat treatment in the acidic medium, but not in the alkaline medium. Neither pepsin nor pronase destroyed the inhibitory function.

Amino Acids↗

PubMed1979

Phaseolus vulgaris isolectin binding to human erythrocytes.

The Phaseolus vulgaris isolectins L4,L3E1, L2E2, L1E3, and E4 were isolated by affinity and ion exchange chromatography. Pure isolectins were radiolabeled by the chloramine-T method with Na125IO4 and their binding to human erythrocytes was studied. A normal erythrocyte has approximately 8 times 10(5) receptor sites for each isolectin; however, the association constants (Ka) of binding increased from 1.1 times 10(7) M-1 to 3.8 times 10(8) M-1, with increasing number of E subunits per tetrameric isolectin molecule. Isolectin to erythrocyte binding reached equilibrium rapidly and was reversed by fetuin. All isolectins competed with 125I-E4 for erythrocyte binding sites, with a constant (KI) similar to the Ka calculated for each respective radiolabeled isolectin. When isolectin binding at 0 degrees C, 4 degrees C, or 8 degrees C was compared to that at 25 degrees C, there was no reduction in the number of binding sites per cell, but the Ka of E4 was reduced to 3 times 10(7) M-1. Fixed erythrocytes displayed similar isolectin binding characteristics.

Binding Sites↗

PubMed1975

Histochemical studies in stomatal apparatus of Phaseolus mungo Linn. I. Localization of enzymes and structural material.

In the present investigations, the localization of several enzymes (Acid Phosphatase, Peroxidase, succinic dehydrogenase, Phosphorylase, alkaline phosphatase, ATP-ase) and other substances in the guard and subsidiary cells as well as trichomes of the leaves of Phaseolus mungo, was carried out. Attempts were also made to follow the sequence of developmental stages starting with meristemoids and culminating in differentiated structures. The basic information thus obtained is used in interpreting the developmental physiology of stomatal differentiation as well as their cellular organisation. Histochemical observations made in the present studies are compared with the electron microscopical observations of Whatley (1972). It is proposed that mitochondria played a basic role in the functioning of the guard cells. The present studies also demonstrated activity of acid phosphatase in the guard cells and was localized in spherosomes. The latter varied in the activity for acid phosphatase and was dependent on the turgid level of the cell. Interestingly, enough localization of phosphatase could only be observed in spherosomes when the osmotic pressure in the cell was relatively low, once the osmotic pressure increased, the activity disappeared.

Acid Phosphatase↗

PubMed1975

Histochemical studies in stomatal apparatus of Phaseolus mungo linn. IV. Mechanism of stomatal action.

The histochemical studies were carried out in the open and closed stomata of Phaseolus mungo leaves. Several enzymes like, Acid phospatase peroxidase, succinic dehydrogenase, phosphorylase, alkaline phosphatase, ATP-ase etc. were localized in the guard and subsidiary cells of epidermal peel. On the basis of cytochemical localization, enzyme activity was precisely interpreted. In the light of fluctuations in the localization, activities of different enzymes, an attempt is made to provide the functional interpretation of stomatal mechanism. We have attempted to correlat our observations in relation to diurnal metabolisms. Our studies suggest that starch-sugar inter-changes played a vital role in the stomatal regulation. We are also inclined to believe that besides guard cells, subsidiary cells also influenced the turgid conditions. A model based on available facts in collaboration with our own studies is presented which tends to explain the stomatal regulation.

Acid Phosphatase↗

PubMed1977

[Purification and properties of the tetrahydropteroylglutamate methyltransferase from green beans (Phaseolus vulgaris) (author's transl)].

The tetrahydropteroylglutamate methyltransferase from green beans (Phaseolus vulgaris) has been purified 80-fold by ion exchange chromatography and gel filtration. Optimal methyl transfer is found at pH 6.5 and 39 degrees C. Even at 0 degrees C, however, a considerable catalytic rate is observed. The Michaelis-Menten constants for homocysteine and 5-methyltetrahydropteroylglutamate are 0.43mM and 2.4 mM, respectively. Magnesium ions enhance the activity. Even purified preparations appear to contain traces of magnesium ions firmly bound, since a residual activity is found without addition of magnesium salts. Though the reaction requires anaerobiosis, an excess of reducing agents is inhibitory. The molecular weight of the transferase, determined by gel filtration, is 40 000 +/- 6%.

5-Methyltetrahydrofolate-Homocysteine S-Methyltran↗