PUROTHIONIN
PUROTHIONIN structure
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Common Name | PUROTHIONIN | ||
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| CAS Number | 9009-72-7 | Molecular Weight | N/A | |
| Density | N/A | Boiling Point | N/A | |
| Molecular Formula | C198H332N68O56S8 | Melting Point | N/A | |
| MSDS | USA | Flash Point | N/A | |
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Expression of the antimicrobial peptides in plants to control phytopathogenic bacteria and fungi.
Plant Cell Rep. 25(6) , 561-72, (2006) Three antimicrobial peptides exhibiting in vitro antifungal activity were expressed in Arabidopsis to compare their in planta activity. Beta-Purothionin, cecropin B, and phor21 were expressed under an endogenous promoter with moderate-level activity and excre... |
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Studies on the inhibition of pancreatic and carboxylester lipases by protamine.
J. Lipid Res. 37(7) , 1481-7, (1996) The basic protein protamine strongly inhibited hydrolysis of triolein emulsified with soybean phosphatidylcholine (PC) by pancreatic and carboxylester lipases; 10 micrograms/ml protamine, about 1000 times lower than the concentration of bovine serum albumin f... |
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Calmodulin binding to alpha 1-purothionin: solution binding and modeling of the complex.
Proteins 14(2) , 127-38, (1992) CD and fluorescence spectroscopic measurements show that calmodulin (CaM) binds to purothionins (alpha 1-purothionin: alpha 1-PT; beta-purothionin: beta-PT) in 1:1 stoichiometry with an affinity similar to that exhibited with the tightest binding CaM-binding ... |
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Characterization of antimicrobial peptides against a US strain of the rice pathogen Rhizoctonia solani.
J. Appl. Microbiol. 97(1) , 169-80, (2004) To identify antimicrobial peptides with high lytic activity against Rhizoctonia solani strain LR172, causal agent of rice sheath blight and aerial blight of soyabeans in the US.Among 12 natural and synthetic antimicrobial peptides tested in vitro, the wheat-s... |
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Characterisation of granulocyte stimulation by thionins from European mistletoe and from wheat.
Biochim. Biophys. Acta 1426(1) , 80-90, (1999) Thionins are small basic peptides found in different plant species, which are known to exert cytotoxic properties. In addition, previous data indicated an activation of human granulocytes by thionins from European mistletoe (viscotoxins, VT). To extend these ... |
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Lipid binding interactions of antimicrobial plant seed defence proteins: puroindoline-a and β-purothionin.
Phys. Chem. Chem. Phys. 13(38) , 17153-62, (2011) The indolines and thionins are basic, amphiphilic and cysteine-rich proteins found in cereals; puroindoline-a (Pin-a) and β-purothionin (β-Pth) are members of these families in wheat (Triticum aestivum). Pin-a and β-Pth have been suggested to play a significa... |
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Mechanism of beta-purothionin antimicrobial peptide inhibition by metal ions: molecular dynamics simulation study.
Biophys. Chem. 121(1) , 30-43, (2006) Wheat beta-purothionin is a highly potent antimicrobial peptide which, however, is inactivated by metal ions. The key structural properties and mechanisms of inhibition of beta-purothionin were investigated for the first time using unconstrained molecular dyn... |
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X-ray scattering studies of model lipid membrane interacting with purothionin provide support for a previously proposed mechanism of membrane lysis.
Eur. Biophys. J. 39(8) , 1155-65, (2010) Thionins, ubiquitous plant toxins, are believed to act by lysing the membrane of pathogenic organisms. Several competing mechanisms were proposed for the lysis of phospholipid membranes by the toxins. In order to study in more detail the proposed mechanisms a... |
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Is there a difference in metal ion-based inhibition between members of thionin family: Molecular dynamics simulation study.
Biophys. Chem. 130(1-2) , 65-75, (2007) Thionins have a considerable potential as antimicrobial compounds although their application may be restricted by metal ion-based inhibition of membrane permeabilizing activity. We previously reported the properties associated with the proposed mechanism of m... |
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Generation of reactive oxygen intermediates (ROI) by the thionins from Viscum album L.
Anticancer Res. 18(6A) , 4291-6, (1998) Extracts from Viscum album L. are widely used as an adjuvant in complementary cancer therapy. While the mechanisms of mistletoe lectin (ML) cytotoxicity are well described, the viscotoxin (VT) effects are unclear at present. Thus, we treated human lymphocytes... |