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PubMed2001

Transmembrane topography of plasma membrane constituents in mung bean (Vigna radiata L.) hypocotyl cells. I. Transmembrane distribution of phospholipids.

The transmembrane distribution of phospholipids (PLs) in the plasma membrane (PM) of mung bean (Vigna radiata L.) hypocotyl cells was investigated using annexin V-fluorescein isothiocyanate, porcine pancreas phospholipase A(2), and (31)P-nuclear magnetic resonance (NMR) spectroscopy. Phosphatidylserine was not located on the cell surface of mung bean protoplasts. However, phosphatidylcholine, phosphatidylethanolamine and phosphatidic acid were found to be almost symmetrically distributed across right-side-out PM vesicles obtained by aqueous two-phase partitioning by porcine pancreas phospholipase A(2) assay. (31)P-NMR assay showed that the amount of PLs is about equal in the outer and the inner leaflets of the right-side-out PM vesicles. These results suggest that the topography of PM PLs might not contribute to well-known asymmetrical properties of the outer and inner surfaces of higher plant PMs. It is also indicated that inside-out PM vesicles created by Brij 58-treatment do not retain the native PL topography on dithionate reduction of 7-nitro-2,1,3-benzoxadiazol-4-yl-labeled PLs incorporated in the PM vesicles.

Cell Membrane↗
PubMed2002

Transmembrane topography of plasma membrane constituents in mung bean (Vigna radiata L.) hypocotyl cells. II. The large scale asymmetry of surface peptides.

The large scale asymmetry in surface (poly)peptides of the plasma membrane (PM) of mung bean (Vigna radiata L.) hypocotyl cells was investigated by protease and 1 M KCl treatments of PM vesicles obtained by an aqueous two-phase partition technique. Proteases only slightly reduced the protein content of right-side-out PM vesicles and the treatment with 1 M KCl resulted in the dissociation of only a few peripheral proteins from the outer surface of right-side-out PM vesicles, indicating that few surface peptides including peripheral proteins existed on the outer surface. From experiments of the re-partitioning of endomembrane vesicles removed from surface peptides, it was found that the surface peptide content is a factor determining the partitioning, and the hypothesis that sterols are asymmetrically distributed across higher plant PM was proposed. We speculate that asymmetrical properties between the outer and the inner surfaces of plant PM, especially in partitioning in the two-phase system, derive from the asymmetry of the bulk of surface peptides and PM sterols. The comparatively low hydrophilicity of the outer surface of the PM would be important for the partitioning of right-side-out PM vesicles in the upper phase of the two-phase system.

Cell Membrane↗
PubMed2004

The Vr-PLC3 gene encodes a putative plasma membrane-localized phosphoinositide-specific phospholipase C whose expression is induced by abiotic stress in mung bean (Vigna radiata L.).

Phosphoinositide-specific phospholipase C (PI-PLC) catalyzes the hydrolysis of phosphatidylinositol 4,5-bisphosphate to generate inositol 1,4,5-trisphosphate and diacylglycerol, both of which act as secondary messengers in animal cells. In this report, we identified in Vigna radiata L. (mung bean) three distinct partial cDNAs (pVr-PLC1, pVr-PLC2, and pVr-PLC3), which encode forms of putative PI-PLC. All three Vr-PLC genes were transcriptionally active and displayed unique patterns of expression. The Vr-PLC1 and Vr-PLC2 transcripts were constitutively expressed to varying degrees in every tissue of mung bean plants examined. In contrast, the Vr-PLC3 mRNA level was very low under normal growth conditions and was rapidly induced in an abscisic acid-independent manner under environmental stress conditions (drought and high salinity). An isolated genomic clone, about 8.2 kb in length, showed that Vr-PLC1 and Vr-PLC3 are in tandem array in the mung bean genome. The predicted primary sequence of Vr-PLC3 (M(r)=67.4 kDa) is reminiscent of the delta-isoform of animal enzymes which contain core sequences found in typical PI-PLCs, such as the catalytic domain comprising X and Y motifs, a lipid-binding C2 domain, and the less conserved EF-hand domain. Results of in vivo targeting experiment using a green fluorescent protein (GFP) showed that the GFP-Vr-PLC3 fusion protein was localized primarily to the plasma membrane of the Arabidopsis protoplast. The C2 domain was essential for Vr-PLC3 to be targeted to the plasma membrane. The possible biological functions of stress-responsive Vr-PLC3 in mung bean plants are discussed.

Amino Acid Sequence↗
PubMed1988

Electrophoretic study of alpha-D-galactosidases from seeds of Glycine soja and Vigna radiata possessing erythroagglutinating activity.

Polyacrylamide gel electrophoresis in an acidic buffer system was used to study the electrophoretic behaviour of two forms of alpha-D-galactosidase from seeds of soy bean (Glycine soja) and mung bean (Vigna radiata). The interaction of the enzymes with saccharides was monitored by affinity electrophoresis; for the preparation of affinity gels, water-soluble O-glycosyl polyacrylamide copolymers and polysaccharides were used. alpha-D-Galactosidases from both sources interact with immobilized alpha-D-galactosyl residues. On the basis of the results of affinity electrophoresis performed in the presence of various free sugars, dissociation constants for the complexes between alpha-D-galactosidase and free sugars were calculated.

Chromatography, Affinity↗
PubMed2003

Cowpea (Vigna unguiculata) vicilins bind to the peritrophic membrane of larval sugarcane stalk borer (Diatraea saccharalis).

In this work, we show that vicilins from two Vigna unguiculata (cowpea) genotypes, Epace-10 and IT 81D-1045, which are susceptible and resistant to attack by the cowpea weevil Callosobruchus maculatus, respectively, associate with the peritrophic membrane (PM) from larvae of Diatraea saccharalis. Solutions with increasing concentrations of vicilins were incubated with PM of the larvae and subsequently analysed by electrophoresis with SDS. It was observed that the majority of the bands of approximately 50,000 Da (characteristic of vicilins) did not appear in the separating gel and only lower molecular weight polypeptides were seen. When vicilins were incubated with PM, and the solution was then heated after the incubation, the band pattern in the gel appeared completely different. It was observed that the vicilins were being hydrolysed by proteinases associated with the PM. When the incubated samples were heated after the reaction, the major bands reappeared, demonstrating that most of the vicilin molecules had bound to the PM of D. saccharalis. These results suggest that when the vicilins are in contact with the PM they are bound and also digested by the PM of this insect. The major and several minor proteinases from the PM were extracted with Triton X-100 and their activity and the inhibition of this activity were analysed by ingel assays. Based on the effects of proteinase inhibitors, the PM-associated activity is due to serine class proteinases. Larvae of D. saccharalis were fed on artificial diets containing purified vicilins from Epace-10 or IT 81D-1045 seeds. Vicilins from Epace-10 did not affect the larval development, while IT 81D-1045 vicilins reduced significantly the survival rate of the sugar cane borer.

Animals↗
PubMed2001

Intraspecific and interspecific competition in Callosobruchus maculatus (F.) and Callosobruchus subinnotatus (Pic) on stored bambara groundnut, Vigna subterranea (L.) Verdcourt.

Intraspecific competition was studied in Callosobruchus maculatus and Callosobruchus subinnotatus. Interspecific competition between the two bruchids was also studied to determine which of these species is likely to cause more damage to stored bambara groundnuts, Vigna subterranea in cases of joint infestation. Results showed that increasing the adult density up to 8 females per 10g of bambara groundnut seeds did not significantly reduce the mean number of eggs laid per female, the number of eggs developing to the adult stage, or the weight of emerged adults of either species. The developmental period of the two species was also not significantly affected. The adult emergence curve of C. maculatus was similar to that of C. subinnotatus and was of the scramble type. C. maculatus performed better than C. subinnotatus in interspecific competition and it achieved this through a higher egg-laying ability and a higher rate of progeny production coupled with a shorter life-cycle. The implications of these findings with respect to damage and possible loss of stored bambara groundnut are discussed.

Journal Article↗
PubMed2003

Effect of lead on growth and nitrate assimilation of Vigna radiata (L.) Wilczek seedlings in a salt affected environment.

The inhibition of seedling growth and nitrate reductase activity in 5 d old Vigna radiata (L.) Wilczek cv. Pusa Baisakhi in the presence of 1.0 mM lead acetate increased drastically, if NaCl (6 and 12 EC) was also present in the nutrient media along with the metal salt. Correspondingly higher endogenous Na+ levels were accumulated in the roots and leaves of seedlings in presence of the two stresses. On the other hand, the levels of endogenous lead get reduced in presence of NaCl in both the roots and leaves. Roots accumulated more Pb2+ and Na+ than the leaves. The two stresses affect more drastically in the additive or even synergistic manner during the early growth phase of the seedlings.

Biomass↗
PubMed2001

Agrobacterium tumefaciens-mediated genetic transformation of mungbean (Vigna radiata L. Wilczek) - a recalcitrant grain legume.

Agrobacterium-mediated transformation of Vigna radiata L. Wilczek has been achieved. Hypocotyl and primary leaves excised from 2-day-old in-vitro grown seedlings produced transgenic calli on B(5) basal medium supplemented with 5x10(-6) M BAP, 2.5x10(-6) M each of 2,4-D and NAA and 50 mg l(-1) kanamycin after co-cultivation with Agrobacterium tumefaciens strains, LBA4404 (pTOK233), EHA105 (pBin9GusInt) and C58C1 (pIG121Hm) all containing beta-glucuronidase (gusA) and neomycin phosphotransferase II (nptII) marker genes. Transformed calli were found resistant to kanamycin up to 1000 mg(.)l(-1). Gene expression of kanamycin resistance (nptII) and gusA in transformed calli was demonstrated by nptII assay and GUS histochemical analysis, respectively. Stable integration of T-DNA into the genome of transformed calli of mungbean was confirmed by Southern blot analysis. Transgenic calli could not regenerate shoots on B(5) or B(5) containing different cytokinins or auxins alone or in combination. However, for the first time, transformed green shoots showing strong GUS activity were regenerated directly from cotyledonary node explants cultured after co-cultivation with LBA4404 (pTOK233) on B(5) medium containing 6-benzylaminopurine (5x10(-7) M) and 75 mg l(-1) kanamycin. The putative transformed shoots were rooted on B(5)+indole-3-butyric acid (5x10(-6) M) within 10-14 days and resulted plantlets subsequently developed flowers and pods with viable seeds in vitro after 20 days of root induction. The stamens, pollen grains and T(0) seeds showed GUS activity. Molecular analysis of putative transformed plants revealed the integration and expression of transgenes in T(0) plants and their seeds.

Journal Article↗
PubMed2000

Analysis of a ferric leghemoglobin reductase from cowpea (Vigna unguiculata) root nodules.

Ferric leghemoglobin reductase (FLbR), an enzyme reducing ferric leghemoglobin (Lb) to ferrous Lb, was purified from cowpea (Vigna unguiculata) root nodules by sequential chromatography on hydroxylapatite followed by Mono-Q HR5/5 FPLC and Sephacryl S-200 gel filtration. The purified cowpea FLbR had a specific activity of 216 nmol Lb(2+)O(2) formed min(-1) mg(-1) of enzyme for cowpea Lb(3+) and a specific activity of 184 nmol Lb(2+)O(2) formed min(-1) mg(-1) of enzyme for soybean Lb(3+). A cDNA clone of cowpea FLbR was obtained by screening a cowpea root nodule cDNA library. The nucleotide sequence of cowpea FLbR cDNA exhibited about 88% similarity with soybean (Glycine max) FLbR and 85% with pea (Pisum sativum) dihydrolipoamide dehydrogenase (DLDH, EC 1.8.1.4) cDNAs. Conserved regions for the FAD-binding site, NAD(P)H-binding site, and disulfide active site were identified among the deduced amino acid sequences of cowpea FLbR, soybean FLbR, pea DLDH and other enzymes in the family of the pyridine nucleotide-disulfide oxido-reductases.

Journal Article↗
PubMed1988

Purification of human erythrocytes specific lectins from rice bean, Phaseolus calcaratus syn. Vigna umbellata, by high-performance liquid chromatography.

Two lectins, an N-acetylgalactosamine-binding lectin, lectin-I, which reacts specifically with human erythrocytes of blood group A, and a galactose-binding lectin, lectin-II, which is specific for human blood group B erythrocytes, have been isolated and purified from rice bean, Phaseolus calcaratus syn. Vigna umbellata, by a salt solubility pH-dependent method, chromatofocusing and high-performance liquid chromatography. The homogeneity of the lectins was determined by liquid chromatography and polyacrylamide gel electrophoresis. The purified lectin-I of molecular mass 80,000 is possibly composed of two subunits of molecular mass ca. 18,000 and 22,000, respectively, whereas lectin-II of molecular mass 100,000 appears to be composed of a monomeric protein of molecular mass 25,000. One endogenous lectin-binding protein was also isolated and purified by liquid chromatography. The endogenous lectin-binding protein of molecular mass 40,000 affects the activity of the A-group specific lectin more than that of the B-group specific lectin. The endogenous lectin-binding protein appears to be composed of a monomeric protein of molecular mass 20,000.

Blood Proteins↗
PubMed2001

Mungbean [Vigna radiata (L.) Wilczek] globulins: purification and characterization.

Vicilin type (8S) and basic 7S globulins and legumin type (11S) globulins were isolated from mungbean [Vigna radiata (L.) Wilczek]. The native molecular weights of the different globulin types were 360000 for legumin, 200000 for vicilin, and 135000 for basic 7S. Some of the 8S globulin apparently complexed and coeluted with the 11S on gel filtration. On SDS-PAGE, 11S was composed of two bands of 40000 and 24000, 8S was composed of 60000, 48000, 32000, and 26000 bands, and basic 7S was composed of 28000 and 16000 bands. The percent composition of total globulins was estimated to be as follow: 8S, 89%; basic 7S, 3.4%; and 11S, 7.6%. The basic 7S and 11S but not the 8S globulins were found to have disulfide bonds. The presence of carbohydrates by conjugated peroxidase reaction was observed in all bands of 8S, the acidic polypeptide of basic 7S, and its complex but not in 11S. The 28000 basic 7S band and its 42000 complex and the first three major bands of 8S cross-reacted with antibodies to all types of soybean conglycinin subunits (alpha, alpha', and beta), whereas the fourth band cross-reacted only with the anti-beta subunit. None of the mungbean globulins cross-reacted with anti-soybean glycinin. Basic 7S was found to be easily extracted with 0.15 M NaCl, 11S was extracted with 0.35 M NaCl,and 8S was extracted over a wide range of NaCl concentrations. The N-terminal sequences of the different subunits/fragments of the globulins were determined and found to have strong homology with storage proteins of other legumes and crops.

Electrophoresis, Polyacrylamide Gel↗
PubMed2004

Characterization of the proteins from Vigna unguiculata seeds.

The proteins from Vigna unguiculata (L.) Walp. (cowpea) seeds were investigated. Globulins constitute over 51% of the total seed protein, with albumins composing approximately 45%. The globulins may be fractionated by native electrophoresis or anion exchange chromatography into three main components, which were termed (in decreasing order of anodic mobility) alpha-vignin, beta-vignin, and gamma-vignin. alpha-Vignin, with a sedimentation coefficient of 16.5S, is a major, nonglycosylated globulin, composed of a major 80 kDa subunit, which upon reduction, produces two polypeptides (20 and 60 kDa). beta-Vignin, with a sedimentation coefficient of 13S, is a major, glycosylated globulin, composed of two main polypeptides (55 and 60 kDa) with no disulfide bonds. Finally, gamma-vignin, a minor globulin, is composed by one main type of subunit (22 kDa), which upon reduction, is converted into a single, apparently heavier polypeptide chain (30 kDa) due to the presence of an internal disulfide bond. Immunological analyses revealed structural homology between beta-vignin and beta-conglutin (the vicilin from Lupinus seeds) but not between alpha- or gamma-vignins and their Lupinus counterparts. Haemagglutination activity toward trypsinized rabbit erythrocytes was found exclusively in the albumin fraction and was strongly inhibited by N-acetylglucosamine or chitin.

Albumins↗
PubMed2003

Functional properties of purified vicilins from cowpea (Vigna unguiculata) and pea (Pisum sativum) and cowpea protein isolate.

The major storage globulins (vicilins) of cowpea (Vigna unguiculata) and pea (Pisum sativum) seeds were purified by ammonium sulfate precipitation, and a semipurified cowpea protein isolate (CPI) was prepared by isoelectric precipitation. Some of the functional properties of these proteins, including solubility, foaming, and emulsifying capacities, were investigated and compared. The solubility of purified cowpea vicilin was reduced at pH 5.0, increasing markedly below and above this value. Pea vicilin exhibited poor solubility between pH 5.0 and pH 6.0, and CPI was little soluble in the pH range from 4.0 to 6.0. At neutral pH, the emulsifying activity indexes (EAI) of purified pea vicilin and CPI were 194 and 291 m(2)/g, respectively, which compare quite favorably to EAIs of 110 and 133 m(2)/g for casein and albumin, respectively. Remarkably, purified cowpea vicilin exhibited an EAI of 490 m(2)/g, indicating a very high emulsifying activity. Purified cowpea and pea vicilins exhibited lower foaming capacities and foam stablity indexes (FSI) than CPI. FSI values of 80 and 260 min were obtained for purified pea and cowpea vicilin, respectively, whereas a FSI value of 380 min was obtained for CPI. These results are discussed in terms of the possible utilization of purified vicilins or protein isolates from pea and cowpea in the food processing industry.

Amino Acids↗
PubMed2005

Detection of proteins related to starch synthase activity in the developing mungbean (Vigna radiata L.).

Proteins associated with starch synthase (SS) activities were identified in immature mungbeans (Vigna radiata L. cv KPS1). Seed soluble extract was separated by native-PAGE and subjected to in situ activity staining. The gel zymogram located starch-enzyme complex bands. The soluble extract was also partitioned by preparative-IEF and screened for SS activity using radioactive assay. IEF fractions eluted within pH 4-6 revealed enriched SS activity of 145-fold. Parallel comparison of the protein profiles among the activity stained enzyme complex and the active isoelectric focused fractions on SDS-PAGE depicted three SS-activity-related proteins with molecular size of 32, 53, and 85 kDa. The 85 kDa protein, however, was identified to be methionine synthase by MALDI-TOF analysis and should be a protein physically associated with the active SS. Polyclonal antibodies raised from eluted native enzyme complex neutralized up to 90% activity and antigenically recognize the other 53 and 32 kDa proteins on Western blot. Antibodies raised from the two individual denatured proteins were able to neutralize SS activities near 60% separately, indicating that the 53 kDa and 32 proteins associated with SS activity are potentially involved in starch biosynthesis during mungbean seed development.

Blotting, Western↗
PubMed2004

Identification of flavonoids in Hakmeitau beans (Vigna sinensis) by high-performance liquid chromatography-electrospray mass spectrometry (LC-ESI/MS).

Liquid chromatography coupled with electrospray mass spectrometry (LC-ESI/MS) with positive and negative ion detection was used for the identification of flavonoids in Hakmeitau beans, a black seed cultivar of cowpea (Vigna sinensis). Gradient elution with water and acetonitrile, both containing 2% formic acid, was employed in chromatographic separation. The peaks were identified by comparison of the retention times and the UV-vis spectroscopic and mass spectrometric data with authentic standards and/or literature data. The identified flavonoids included six anthocyanins (cyanidin 3-O-galactoside, cyanidin 3-O-glucoside, delphinidin 3-O-glucoside, malvidin 3-O-glucoside, peonidin 3-O-glucoside, and petunidin 3-O-glucoside) and four flavonol/flavonol glycosides (kaempferol 3-O-glucoside, quercetin, quercetin 3-O-glucoside, and quercetin 3-O-6' '-acetylglucoside). The tentatively identified flavonoids included two anthocyanins (malvidin 3-O-acetylglucoside and peonidin 3-O-malonylglucoside) and three flavonol glycosides (myricetin-3-O-glucoside, quercetin 7-O-glucoside, and quercetin-3-O-diglucoside). These flavonoids are present in seed coats, and the contents of anthocyanins and flavonol glycosides were 20.7 and 2.0 mg/g, respectively.

Anthocyanins↗
PubMed2005

Effect of processing on the antioxidant vitamins and antioxidant capacity of Vigna sinensis Var. Carilla.

Cowpea (Vigna sinensis L. var. Carilla) flours obtained by fermentation with inoculum Lactobacillus plantarum (PF) or with the natural microorganisms present in the flour (NF) and subsequent heat treatment in an autoclave were prepared to study the effect of fermentation on the antioxidant vitamin content and on the antioxidant capacity. Bacterial counts and pH values, vitamins C and E, carotenoids, glutathione (GSH), superoxide dismutase-like activity (SOD-like activity), peroxyl radical-trapping capacity (PRTC), lipid peroxidation in unilamillar liposomes, and Trolox equivalent antioxidant capacity (TEAC) were evaluated in raw and processed cowpea flours. gamma-Tocopherol and delta-tocopherol were found in raw cowpea, whereas vitamin C and carotenoids were not detected. An increase in the vitamin E activity was observed in PF, whereas vitamin C and carotenoids were not detected in fermented cowpea flours. Fermentation or heat treatment in an autoclave after fermentation produced processed cowpea flours with lower PRTC, glutathione content, and SOD-like activity than those of the raw seeds. However, those processes increased the capacity to inhibit the lipid peroxidation in unilamellar lipoposomes and TEAC. According to the results obtained in this study, the fermentation of cowpeas (naturally or with L. plantarum) and fermentation and subsequent heat treatment in an autoclave are good processes to obtain functional cowpea flours having higher antioxidant capacity than the raw legume.

Antioxidants↗
PubMed2005

The identification of starch phosphorylase in the developing mungbean (Vigna radiata L.).

Starch phosphorylase (SP) in immature mungbean (Vigna radiata L. cv KPS1) seed soluble extract was detected by in situ activity staining and identified by MALDI-TOF mass analysis. After in situ SP assay on native-PAGE, a major starch-enzyme complex was located on the gel zymogram in a dose-dependent manner. This complex depicted two major SP-activity related proteins, 105 kDa and 55 kDa, by SDS-PAGE. The mass and predicted sequence of the tryptic fragments of the isolated 105 kDa protein, analyzed by MALDI-TOF spectroscopy and bioinformatic analysis, confirmed it to be mungbean SP as a result of high similarity to the L-SP of known plant. Polyclonal antibodies raised from the 55 kDa recognized both the 105 kDa and the 55 kDa proteins on the Western blot and neutralized partial SP activity, indicating that the two proteins were immunologically related. The 55 kDa protein possess high similarity to the N-terminal half of the 105 kDa SP was further confirmed. The SP activity and the activity stained protein density in mungbean soluble extract decreased as the seed size increased during early seed growth. These data indicate that mungbean 105 kDa SP and SP activity-related 55 kDa were identified in the developing mungbean.

Amino Acid Sequence↗