Your browser doesn't support javascript.
loading
Show: 20 | 50 | 100
Results 1 - 10 de 10
Filter
1.
Folia Microbiol (Praha) ; 53(4): 351-5, 2008.
Article in English | MEDLINE | ID: mdl-18759120

ABSTRACT

The root nodules of Phaseolus mungo (a herbaceous leguminous pulse) contained a high amount of 3-indolylacetic acid (IAA). A tryptophan pool present in the nodule might play the role of precursor for IAA production. From the root nodule a Rhizobium sp. was isolated. The symbiont produced a large amount of IAA (142 microg/mL) from L-tryptophan-supplemented basal medium. The production of IAA by the symbiont was much increased over the control when a L-tryptophan (2 mg/mL) supplemented C-free mineral medium was enriched with mannitol (1 %), L-asparagine (0.3 %) and thiamine hydrochloride (1 microg/mL). The possible role of the rhizobial production of IAA on the rhizobia-legume symbiosis is discussed.


Subject(s)
Indoleacetic Acids/metabolism , Phaseolus/microbiology , Rhizobium/metabolism , Root Nodules, Plant/metabolism , Culture Media/metabolism , Phaseolus/metabolism , Rhizobium/growth & development , Rhizobium/isolation & purification , Root Nodules, Plant/microbiology
2.
Curr Microbiol ; 56(5): 495-8, 2008 May.
Article in English | MEDLINE | ID: mdl-18228096

ABSTRACT

The root nodules of Phaseolus mungo (L.), a herbaceous leguminous pulse, contain high amounts of ascorbic acid (AsA). A glucose pool present in the nodule might serve as precursor for AsA production. From root nodule, a Rhizobium sp. was isolated. The symbiont produced a large amount of AsA (290.5 microg/ml) from glucose-supplemented basal medium. The production of AsA by the symbiont was much greater than that of the control when the glucose (0.5%)-supplemented mineral medium was enriched with thiamine hydrochloride (20 microg/100 ml), biotin (20 microg/100 ml), and L-asparagine (0.2%). The possible role of the rhizobial production of AsA on rhizobia-legume symbiosis is discussed.


Subject(s)
Ascorbic Acid/metabolism , Phaseolus , Rhizobium/metabolism , Root Nodules, Plant , Phaseolus/metabolism , Phaseolus/microbiology , Root Nodules, Plant/metabolism , Root Nodules, Plant/microbiology , Symbiosis
3.
Indian J Exp Biol ; 40(7): 796-801, 2002 Jul.
Article in English | MEDLINE | ID: mdl-12597549

ABSTRACT

The Rhizobium sp. isolated from healthy and mature root nodules of a leguminous tree, Dalbergia lanceolaria Linn. f., preferred mannitol and KNO3 for growth as carbon and nitrogen sources, respectively. The bacterium produced a high amount (22.3 microg/ml) of indole acetic acid (IAA) from L-tryptophan supplemented basal medium. Growth and IAA production started simultaneously. IAA production was maximum at 20 hr when the bacteria reached the stationary phase of growth. Cultural requirements were optimized for maximum growth and IAA production. The IAA production by the Rhizobium sp. was increased by 270.8% over control when the medium was supplemented with mannitol (1%,w/v), SDS (1 microg/ml), L-asparagine (0.02%,w/v) and biotin (1 microg/ml) in addition to L-tryptophan (2.5 mg/ml). The possible role of IAA production in the symbiosis is discussed.


Subject(s)
Fabaceae/microbiology , Indoleacetic Acids/metabolism , Plant Roots/microbiology , Rhizobium/growth & development , Rhizobium/metabolism
4.
Indian J Exp Biol ; 39(2): 155-9, 2001 Feb.
Article in English | MEDLINE | ID: mdl-11480212

ABSTRACT

The Azorhizobium caulinodans isolated from the stem nodules of a leguminous emergent hydrophyte, Aeschynomene aspera, produced a large amount of extracellular polysaccharides (EPS) in yeast extract basal medium. Maximum EPS production was at the stationary phase of growth. EPS production was increased by 919% over control when the medium was supplemented with sucrose (1.5%), D-biotin (1 microgram/ml) and casamino acid (0.1%). EPS contained rhamnose and arabinose. Possible role of the azorhizobial EPS production in the stem nodule symbiosis is discussed.


Subject(s)
Fabaceae/metabolism , Fabaceae/microbiology , Plant Stems/microbiology , Plants, Medicinal , Polysaccharides, Bacterial/biosynthesis , Rhizobium/metabolism , Rhizobium/isolation & purification
5.
Microbiol Res ; 155(2): 123-7, 2000 Jul.
Article in English | MEDLINE | ID: mdl-10950195

ABSTRACT

A Rhizobium sp. isolated from the root nodules of a leguminous pulse-yielding shrub, Cajanus cajan, was found to produce high amounts (99.7 microg/ml) of indole acetic acid (IAA) during growth in basal medium supplemented with L-tryptophan. The Rhizobium sp. was a fast growing species which reached its stationary phase at 28 h. The IAA production could be increased upto 653.3% over control by supplementing the carbon-free incubation medium with glucose (5 g/l), NiCl2 (10 microg/ml) and glutamic acid (0.5 g/l). The possible role of rhizobial IAA on the rhizobia-legume symbiosis is discussed.


Subject(s)
Fabaceae/microbiology , Indoleacetic Acids/metabolism , Plant Growth Regulators/metabolism , Plants, Medicinal , Rhizobium/metabolism , Symbiosis , Plant Roots/metabolism , Plant Roots/microbiology , Rhizobium/growth & development
6.
Acta Microbiol Immunol Hung ; 44(2): 109-18, 1997.
Article in English | MEDLINE | ID: mdl-9330659

ABSTRACT

The Rhizobium sp. isolated from the root nodules of Desmodium gangeticum DC. produced a high amount of indole acetic acid (IAA) from tryptophan in culture. For maximum IAA production, the bacteria preferred L-isomer over DL- or D-isomer of tryptophan. The production of IAA could be increased up to 37% over yeast extract ribose medium by supplementing the medium with ZnSO4 (0.1 microgram/ml), asparagine (0.1%) and nicotinic acid (0.1 microgram/ml). The possible relationship between the rhizobial IAA production and legume-rhizobia symbiosis is discussed.


Subject(s)
Fabaceae/microbiology , Indoleacetic Acids/metabolism , Plants, Medicinal , Rhizobium/metabolism , Rhizobium/growth & development
7.
Indian J Biochem Biophys ; 33(6): 491-7, 1996 Dec.
Article in English | MEDLINE | ID: mdl-9219435

ABSTRACT

A trypsin like serine-proteinase of M(r) 16,000 Da, optimally active at pH 8.4 on N-benzoyl-arginine ethyl ester (BAEE) was purified from 4-day old germinated seeds of rice bean, Vigna umbellata (Thunb), by ammonium sulphate precipitation, gel filtration, ion-exchange chromatography and by high performance liquid chromatography (HPLC). The purity of the enzyme was checked by polyacrylamide gel electrophoresis (PAGE). The enzyme activity was studied on natural substrates like casein, haemoglobin and vicilin, a rice bean storage protein. The activity of the enzyme was completely inhibited by phenylmethylsulfonyl fluoride, but not by iodoacetamide and HgCl2, suggesting it to be a serine protease. Loss of activity in presence of EDTA was reversed by addition of Ca2+.


Subject(s)
Fabaceae/enzymology , Plants, Medicinal , Serine Endopeptidases/isolation & purification , Serine Endopeptidases/metabolism , Calcium/pharmacology , Chromatography, High Pressure Liquid , Chromatography, Ion Exchange , Edetic Acid/pharmacology , Electrophoresis, Polyacrylamide Gel , Enzyme Inhibitors/pharmacology , Kinetics , Substrate Specificity , Temperature
8.
J Chromatogr ; 431(1): 37-44, 1988 Sep 23.
Article in English | MEDLINE | ID: mdl-3235536

ABSTRACT

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.


Subject(s)
Erythrocytes/analysis , Fabaceae/analysis , Lectins/isolation & purification , Plants, Medicinal , Blood Proteins/analysis , Carbohydrates/analysis , Chromatography, High Pressure Liquid , Electrophoresis, Polyacrylamide Gel , Hemagglutination Inhibition Tests , Hemagglutination Tests , Humans , Indicators and Reagents , Isoelectric Focusing , Molecular Weight , Plant Lectins
9.
Biochem J ; 251(1): 195-9, 1988 Apr 01.
Article in English | MEDLINE | ID: mdl-3390154

ABSTRACT

Vicia faba lectin contained 40-57% beta-conformation, 4-23% alpha-conformation along with random coil at pH 7.2 depending upon the analytical methods used. The percentage of beta-conformation increased with the addition of N-acetyl-D-glucosamine or methyl alpha-D-mannopyranoside. The structural transitions of V. faba lectin were affected by alkali at pH 9.6 and 10.6. Binding constants and free energy changes for the interaction between V. faba lectin and N-acetyl-D-glucosamine and methyl alpha-D-mannopyranoside were estimated at pH 7.2 using the c.d. and fluorescence methods.


Subject(s)
Acetylglucosamine/metabolism , Fabaceae/metabolism , Glucosamine/analogs & derivatives , Lectins/metabolism , Methylglycosides/metabolism , Methylmannosides/metabolism , Plants, Medicinal , Circular Dichroism , Kinetics , Macromolecular Substances , Plant Lectins , Protein Conformation , Spectrometry, Fluorescence , Thermodynamics
10.
Biochem J ; 197(3): 751-3, 1981 Sep 01.
Article in English | MEDLINE | ID: mdl-7325983

ABSTRACT

A D-galactose-binding lectin agglutinating human erythrocytes has been purified from the seeds of the Indian coral tree (Erythrina variegata (Linn.) var. orientalis (Linn.) Merrill] by affinity chromatography on acid-treated Sepharose-6B gel. It has a higher reactivity for O-group erythrocytes. The lectin is a glycoprotein having a leucoagglutinating property.


Subject(s)
Carrier Proteins/isolation & purification , Erythrina/analysis , Lectins/isolation & purification , Plants, Medicinal , Carrier Proteins/pharmacology , Chromatography, Affinity , Galectins , Hemagglutination/drug effects , Lectins/pharmacology , Plant Lectins , Seeds/analysis , Trees
SELECTION OF CITATIONS
SEARCH DETAIL