Isolation of the virus inhibitor from the root extract of Boerhaavia diffusa inducing systemic resistance in plants

1979 ◽  
Vol 57 (11) ◽  
pp. 1214-1217 ◽  
Author(s):  
H. N. Verma ◽  
L. P. Awasthi ◽  
K. C. Saxena
Keyword(s):  
Molecular Weight ◽  
Organic Solvents ◽  
Preliminary Analysis ◽  
Antiviral Agent ◽  
Systemic Resistance ◽  
Partial Purification ◽  
Root Extract ◽  
Virus Inhibitor ◽  
Boerhaavia Diffusa

An antiviral agent, active against spherical and tubular viruses in hypersensitive and systemic hosts, has been isolated from the roots of Boerhaavia diffusa. Partial purification of inhibitor by organic solvents, Sephadex gel, and protein precipitants has been achieved. Preliminary analysis indicates that the inhibitor may be a glycoprotein with a molecular weight of 16 000–20 000 daltons.

Antiviral activity of Boerhaavia diffusa root extract and the physical properties of the virus inhibitor

1979 ◽  
Vol 57 (8) ◽  
pp. 926-932 ◽  
Author(s):  
H. N. Verma ◽  
L. P. Awasthi
Keyword(s):  
Antiviral Activity ◽  
Trichloroacetic Acid ◽  
Host Plants ◽  
Room Temperature ◽  
Actinomycin D ◽  
Root Extract ◽  
Virus Inoculation ◽  
Positive Identification ◽  
Virus Inhibitor ◽  
Boerhaavia Diffusa

The aqueous extract of air-dried roots of Boerhaavia diffusa shows broad-spectrum antiviral activity and no phytoxic effects. Infection by four viruses was completely prevented, at treated and nontreated sites, when the extract was applied on two basal leaves of host plants 24 h prior to virus inoculation. This inhibition was completely reversed by the application of actinomycin D on treated leaves within 6 h of extract treatment and partially reversed within 18 h. The crude extract from resistant leaves contained an inhibitor of virus infection.The inhibitor in the root extract was partially active up to a dilution of 1:500, was completely inactivated at 95 °C for 10 min, and survived at room temperature for 20 days. The expression of inhibitory activity was prevented when the treated plants were exposed to temperatures beyond 35 °C. The inhibitory principle in the extract was nondialyzable and insoluble in organic solvents, viz., petroleum ether, solvent ether, chloroform, and benzene. It was adsorbed by animal charcoal, wood charcoal, and celite, and was precipitated by ammonium sulphate (90%), ethanol (50%), and cold trichloroacetic acid (10%). The inhibitor was not sedimented at 120 000 × g for 120 min. Further characterization is being done for positive identification of the inhibitor.

Occurrence of a highly antiviral agent in plants treated with Boerhaavia diffusa inhibitor

1980 ◽  
Vol 58 (20) ◽  
pp. 2141-2144 ◽  
Author(s):  
H. N. Verma ◽  
L. P. Awasthi
Keyword(s):  
Plant Species ◽  
Plant Cells ◽  
Antiviral Agent ◽  
Root Extract ◽  
Highly Active ◽  
Naturally Occurring ◽  
Virus Content ◽  
Boerhaavia Diffusa

A naturally occurring glycoprotein present in Boerhaavia diffusa root extract (BD inhibitor), causes plant cells to produce a highly active antiviral agent (AVA) that defends cells against infection by viruses. AVA was present in inhibitor-treated plants only, but not in nontreated plants, and was produced 2–48 h after treatment with BD inhibitor. AVA was effective not only in plant species in which it was produced but in other plant species as well. Crude AVA was active both in vitro and in vivo. In vitro, it markedly reduced the infectivity of viruses, and in vivo, the virus content in AVA-treated leaves and leaf discs was considerably suppressed. The AVA showed the characteristics of protein.

Extraction and Partial Purification of Protease from Bilimbi (Averrhoa bilimbi L.)

2013 ◽  
Vol 10 (2) ◽  
pp. 29
Author(s):  
Normah Ismail ◽  
Nur' Ain Mohamad Kharoe
Keyword(s):  
Molecular Weight ◽  
Protein Content ◽  
Ammonium Sulfate ◽  
Molecular Weight Distribution ◽  
Weight Distribution ◽  
Protease Activity ◽  
Protein Concentration ◽  
Temperature Stability ◽  
Partial Purification ◽  
Ammonium Sulfate Precipitation

Unripe and ripe bilimbi (Averrhoa bilimbi L.) were ground and the extracted juices were partially purified by ammonium sulfate precipitation at the concentrations of 40 and 60% (w/v). The collected proteases were analysed for pH, temperature stability, storage stability, molecular weight distribution, protein concentration and protein content. Protein content of bilimbi fruit was 0.89 g. Protease activity of both the unripe and ripe fruit were optimum at pH 4 and 40°C when the juice were purified at 40 and 60% ammonium sulfate precipitation. A decreased in protease activity was observed during the seven days of storage at 4°C. Molecular weight distribution indicated that the proteases protein bands fall between IO to 220 kDa. Protein bands were observed at 25, 50 and 160 kDa in both the unripe and ripe bilimbi proteases purified with 40% ammonium sulfate, however, the bands were more intense in those from unripe bilimbi. No protein bands were seen in proteases purified with 60% ammonium sulfate. Protein concentration was higher for proteases extracted with 40% ammonium sulfate at both ripening stages. Thus, purification using 40% ammonium sulfate precipitation could be a successful method to partially purify proteases from bilimbi especially from the unripe stage. 

Partial purification of a boar sperm membrane protein inducing sperm agglutinating antibody

1990 ◽  
Vol 10 (2) ◽  
pp. 131-139
Author(s):  
Oyewole Adeyemo ◽  
E. O. Okegbile ◽  
O. O. Olorunsogo
Keyword(s):  
Molecular Weight ◽  
Membrane Protein ◽  
Gel Electrophoresis ◽  
Sodium Dodecyl ◽  
Gel Filtration ◽  
Partial Purification ◽  
Boar Sperm ◽  
Sperm Membrane ◽  
Triton X

For the development of immunological contraception, attention is being concentrated on the possibility of using a sperm membrane antigen. Boar sperm membrane was extracted with triton-X 100 and fractionated by Sephadex G-150 column chromatography. The glycosylated and nonglycosylated portions of protein peaks from the gel filtration were obtained by fractionating on concanavalin A-Sepharose and eluting the bound protein with 0.3 M methyl mannoside. A glycosylated fraction was found to induce sperm agglutinating antibodies in rabbit. The partially purified protein has a molecular weight of 30 kilodaltons, as determined by sodium dodecyl polyaccyrlamide gel electrophoresis. Further work is planned on the histochemical determination of the origin of this protein and species cross-activity of the antibody.

scholarly journals Toxicity of Thevetia peruviana (Pers) Schum. Extract to Adults of Callosobruchus maculatus F. (Coleoptera: Bruchidae)

1970 ◽  
pp. 105-109 ◽  
Author(s):  
JU Mollah ◽  
W Islam
Keyword(s):  
Ethyl Acetate ◽  
Key Words ◽  
Organic Solvents ◽  
Callosobruchus Maculatus ◽  
Root Extract ◽  
Thevetia Peruviana

Leaf, stem and roots of Thevetia peruviana (Pers) Schum. were extracted in four organic solvents; petroleum spirit, ethyl acetate, acetone and methanol and tested against the adults of Callosobruchus maculatus F. All the tested extracts effectively produced mortality of C. maculatus and their toxicity was in order of solvents: petroleum spirit>ethyl acetate>acetone>methanol. Root extract was the most toxic to C. maculatus. Females were more tolerant than males. Key words: Extract, mortality, solvent, Thevetia peruviana, Callosobruchus maculatus. DOI = 10.3329/jard.v5i1.1466 J Agric Rural Dev 5(1&2), 105-109, June 2007

Enzymatic sulfation of steroids. V. Partial purification and some properties of sulfotransferase III, the major glucocorticoid sulfotransferase of liver cytosols from male rats

1978 ◽  
Vol 56 (11) ◽  
pp. 1028-1035 ◽  
Author(s):  
Sanford S. Singer ◽  
James Gebhart ◽  
Edward Hess
Keyword(s):  
Molecular Weight ◽  
Sulfhydryl Groups ◽  
Male Rats ◽  
Partial Purification ◽  
Ph Optimum ◽  
Fold Enrichment ◽  
Competitive Inhibitors ◽  
Sequential Mechanism ◽  
Inhibition Studies ◽  
Estradiol 17Β

This manuscript describes purification of sulfotransferase III (STIII), the major hepatic glucocorticoid sulfotransferase of male rats, 77.8 ± 16 fold from cytosol. This represents a probable 250–345 fold enrichment, compared with homogenates. Purified STIII has a molecular weight of 61 500 ± 2500 from Sephadex G-100 chromatography. It is markedly activated by 5 mM divalent Ba, Ca, Co, Cr, Mg, Mn, and Ni salts; inhibited strongly by 5 mM divalent Zn and Cd; and unaffected by 8 mM ADP, ATP, and AMP. Comparison of the ability of purified STIII to sulfate equimolar Cortisol, estradiol-17β, testosterone, and dehydroepiandrosterone suggests that the enzyme may sulfate glucocorticoids preferentially. However, its Cortisol sulfotransferase activity is inhibited by a variety of steroids. Of these, dehydroepiandrosterone, dexamethasone, and progesterone were tested extensively. They were found to be competitive inhibitors. STIII has a sharp pH optimum at pH 6.0 ± 0.1. However, it is routinely assayed at pH 6.8, as explained in the text. It exhibits a sequential mechanism and Km values of 6.82 ± 1.2 and 6.28 ± 0.64 μM for Cortisol and 3′-phosphoadenosine-5′-phosphosulfate, respectively. It also possesses essential sulfhydryl groups, as shown by p-hydroxymercuribenzoate inhibition studies.

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