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At least 19 recordsLinked to original sources
PubMed1979

Specific interaction of human Tamm-Horsfall gylcoprotein with leucoagglutinin, a lectin from Phaseolus vulgaris (red kidney bean).

Human Tamm-Horsfall glycoprotein inhibits lymphocyte transformation induced by leucoagglutinin and haemagglutinin from Phaseolus vulgaris (red kidney bean). The glycoprotein interacts with the two lectins, giving insoluble precipitates. The interaction with leucoagglutinin is highly specific, and the shape of the precipitin curve is that of an antigen-antibody reaction; precipitation is specifically inhibited by N-acetyl-D-galactosamine. Results are discussed, and it is suggested that inhibition of lymphocyte transformation is due to competition between human Tamm-Horsfall glycoprotein and carbohydrate receptors on lymphocytes for the two lectins. The interaction between human Tamm-Horsfall glycoprotein and Phaseolus vulgaris lectins has been used to develop a one-step procedure for the separation of the two lectins by affinity chromatography on (human Tamm-Horsfall-glycoprotein)-Sepharose.

Acetylglucosamine↗
PubMed2026

Genomic resources to advance seed coat color and patterning genetics and breeding in common bean (Phaseolus vulgaris L.).

Seed coat color and patterning are key quality traits in common bean (Phaseolus vulgaris L.) that define market classes and strongly influence consumer preference and market value. These traits are controlled by a complex network of major genes (sometimes with epistatic interactions), which complicates the recovery of desired market class phenotypes following inter-market class hybridization. Although many of the underlying loci have been genetically mapped, diagnostic, high-throughput molecular markers for efficient allele tracking across the Middle American and Andean gene pools remain limited. In this study, we developed and validated 24 gene-specific PCR Allele Competitive Extension (PACE) markers targeting seven major seed coat color genes (G, B, V, J, Rk, T, and Z) and two patterning genes (CPi and CSt), together with a previously reported marker associated with the postharvest seed coat darkening locus (Psd). An additional PACE marker targeting the Phaseolin (Phs) locus was developed to distinguish Middle American (S-type) and Andean (T-type) gene pools, providing a complementary tool for assessing genetic background alongside seed coat-specific loci. Marker performance was evaluated across three diverse panels, revealing high diagnostic accuracy for most loci (90%-100%). However, for loci such as J, V, Rk, T, and Z, allele-specific markers or marker combinations were required to capture full allelic diversity. Haplotype analysis further revealed substantial allelic diversity across market classes and identified background-specific interactions. Collectively, these results provide a comprehensive set of high-resolution, gene-anchored PACE markers for seed coat color, patterning, and gene pool classification in common bean. These markers enable rapid and precise allele tracking in breeding populations and germplasm collections, facilitating marker-assisted selection for market class-specific seed coat traits and accelerating genetic improvement.

Phaseolus↗
PubMed1976

Characterization, enzymatic and lectin properties of isolated membranes from Phaseolus aureus.

Cellular membranes were prepared from the non-extending part of dark grown hypocotyls of Phaseolus aureus. The relative effectiveness of continuous and discontinuous sucrose gradient centrifugation for the separation of membranes was investigated. Characteristic densities of membranes were determined by the localization of enzyme activities on continuous sucrose gradients: NADH-cytochrome c-reductase for endoplasmic reticulum, beta-1-3-glucan synthetase for plasma-membrane and IDPase for dictyosomes. The difficulties involved in the application of ATPase and IDPase as specific membrane markers are discussed. Negative staining of isolated fractions indicated that intact dictyosomes could be prepared from this tissue without the use of chemical fixatives in the homogenization medium. Extraction of isolated membranes showed that carbohydrate-binding proteins (lectins) were present both in an easily removable and in a more strongly bound form. In vivo incorporation of D-[U-14C]glucose and subsequent isolation and solubilization of the different membranes showed that sugar-containing polymers could be released without hydrolytic techniques and were present in the equivalent extracts that exhibited lectin activity. The possibility of lectin-polysaccharide complexes in endoplasmic reticulum and dictyosomes and their involvement in the synthesis and transport of secretory substances by the membranes is discussed.

Adenosine Triphosphatases↗
PubMed1975

SH-proteinase from bean Phaseolus vulgaris var. Perlicka.

An SH-proteinase (EC 3.4.22.-) has been isolated from beans of the species Phaseolus vulgaris var. Perlicka. The enzyme is homogeneous when subjected to disc electrophoresis, electrofocusing and sedimentation analysis. The molecular weight was determined as 26,000-28,000 by gel filtration, 30,850 +/- 1500 by sedimentation analysis and 26,930-27,410 by calculation from the amino acid composition (Lys20-21, His3, Arg9, Asp21-22, Thr13, Ser18, Pro12-13, Glu23-24, Gly30, Ala16, Cys/29, Val19, Met1, Ile10, Leu13, Tyr14, Phe6, Trp3). The N-terminal amino acid of the proteinase is isoleucine. The effect of concentration, time of hydrolysis, pH, temperature, cations, anions, urea and guanidine - HCl on the proteolytic activity of the SH-proteinase was studied.

Amino Acids↗
PubMed1978

The chemical modification of tryptophan residues of alpha-mannosidase from Phaseolus vulgaris.

Reaction of alpha-mannosidase (alpha-D-mannoside mannohydrolase, EC 3.2.1.24) from Phaseolus vulgaris with N-bromosuccinimide or 2-hydroxy-5-nitrobenzyl bromide- resulted in loss of enzyme activity. Spectral absorption and fluorescence studies, as well as amino acid analysis, suggested that only tryptophan residues had been modified. No change in conformation could be detected by density gradient ultracentrifugation or circular dichroism of alpha-mannosidase modified by N-bromosuccinimide to virtually zero enzyme activity. The inhibition was partly offset by the substrate analogue alpha-methyl-D-mannoside and the competitive inhibitor mannono-1,4-lactone. Concomitantly, two tryptophan residues fewer were oxidized per molecule. After modification V was reduced, while Km seemed unchanged. Further, there was found evidence for the enzyme having a secondary structure dominated by beta-pleated sheets.

2-Hydroxy-5-nitrobenzyl Bromide↗
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↗
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↗
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↗
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↗
PubMed1975

Purification and properties of phaseolamin, an inhibitor of alpha-amylase, from the kidney bean, Phaseolus vulgaris.

Kidney beans, Phaseolus vulgaris, contain a proteinaceous inhibitor of alpha-amylase, which we have named phaseolamin. The inhibitor has been purified to homogeneity by conventional protein fractionation methods involving heat treatment, dialysis, and chromatography on DEAE-cellulose, Sephadex G-100, and CM-cellulose. Phaseolamin is specific for animal alpha-amylases, having no activity towards the corresponding plant, bacterial, and fungal enzymes, or any other hydrolytic enzyme tested. Optimal inhibitory activity is expressed during preincubation of enzyme and inhibitor at pH 5.5 and 37 degrees. Substrate prevents inhibition. Measurement of the stoichiometry on inhibition showed that a 1:1 complex of alpha-amylase and inhibitor is formed. Complex formation was demonstrated by chromatography on Sephadex G-100. The phaseolamin-amylase complex is dissociated at low pH values, apparently as a result of destruction of the enzyme; the complex cannot be dissociated by other conditions unfavorable for inhibition (low temperature or high pH). Phaseolamin inhibits hog pancreatic alpha-amylase in a noncompetitive manner.

Amylases↗
PubMed1979

[Comparison of glutamate dehydrogenase and glutamine synthetase activities in the roots and aerial organs of an obligate halophyte: Suaeda maritima var. macrocarpa and a glycophyte: Phaseolus vulgaris, grown in presence of different concentration of NaCl].

The glutamate dehydrogenase and glutamine synthetase activities of an obligate halophyte, Suaeda maritima var. macrocarpa and a glycophyte. Phaseolus vulgaris are compared in function of salinity (increasing concentrations of NaCl) of the culturing solution. In culture, addition of NaCl stimulates glutamine synthetase activity and lowers glutamine dehydrogenase activity in the aerial organs and in the roots of Suaeda as opposed to what is observed in the glycophyte. Hence the obligatory halophily of Suaeda is related to an increase of the glutamine synthetase activity in a sal-trich medium corresponding to the stimulation of nitrate reductase and proteogenesis.

Glutamate Dehydrogenase↗