scholarly journals Purification and partial characterization of another form of the antiviral protein from the seeds of Phytolacca americana L. (pokeweed)

1982 ◽  
Vol 203 (1) ◽  
pp. 55-59 ◽  
Author(s):  
L Barbieri ◽  
G M Aron ◽  
J D Irvin ◽  
F Stirpe

1. The pokeweed antiviral protein, previously identified in two forms (PAP and PAP II) in the leaves of Phytolacca americana (pokeweed) [Obrig. Irvin & Hardesty (1973) Arch. Biochem. Biophys. 155, 278-289; Irvin, Kelly & Robertus (1980) Arch. Biochem. Biophys. 200, 418-425] is a protein that prevents replication of several viruses and inactivates ribosomes, thus inhibiting protein synthesis. 2. PAP is present in several forms in the seeds of pokeweed. One of them, which we propose to call ‘pokeweed antiviral protein from seeds’ (PAP-S) was purified in high yield (180 mg per 100 g of seeds) by chromatography on CM-cellulose, has mol.wt. 30 000, and is similar to, but not identical with. PAP and PAP II. 3. PAP-S inhibits protein synthesis in a rabbit reticulocyte lysate with an ID50 (concentration giving 50% inhibition) of 1.1 ng/ml (3.6 × 10(-11) M), but has much less effect on protein synthesis by whole cells, with an ID50 of 1 mg/ml (3.3 × 10(-5) M), and inhibits replication of herpes simplex virus type 1.

1989 ◽  
Vol 257 (3) ◽  
pp. 801-807 ◽  
Author(s):  
L Barbieri ◽  
A Bolognesi ◽  
P Cenini ◽  
A I Falasca ◽  
A Minghetti ◽  
...  

1. Ribosome-inactivating proteins were found in high amounts in one line of cells of Phytolacca americana (pokeweed) cultured in vitro and, in less quantity, in lines of Saponaria officinalis (soapwort) and of Zea mays (corn) cells. 2. The main ribosome-inactivating protein from pokeweed cells was purified to homogeneity. It is a protein with Mr 29,000 and basic pI, similar to the ‘pokeweed antiviral protein’ (PAP), a ribosome-inactivating protein from pokeweed leaves. We propose to call the pokeweed antiviral protein isolated from pokeweed cells PAP-C. 3. PAP-C inactivates ribosomes in a less-than-equimolar ratio, thus inhibiting protein synthesis by a rabbit reticulocyte lysate with an IC50 (concentration causing 50% inhibition) of 0.067 nM (2 ng/ml), and modifies rRNA in a manner apparently identical to that of ricin and other ribosome-inactivating proteins. It inhibits protein synthesis by intact cells with an IC50 of 0.7-3.4 microM, and is toxic to mice with an LD50 of 0.95 mg/kg.


1991 ◽  
Vol 20 (1) ◽  
pp. 71-83
Author(s):  
Edward F. Arko ◽  
Jasmine I. Daksis ◽  
Voon-Loong Chan

2012 ◽  
Vol 3 ◽  
Author(s):  
Yoshifumi Muto ◽  
Fumi Goshima ◽  
Yoko Ushijima ◽  
Hiroshi Kimura ◽  
Yukihiro Nishiyama

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