scholarly journals Oral treatment of transmissible gastroenteritis with natural human interferon alpha: A field study

1995 ◽  
Vol 45 (3-4) ◽  
pp. 355-360 ◽  
Author(s):  
Joseph M. Cummins ◽  
Richard E. Mock ◽  
Bradford W. Shive ◽  
Steven Krakowka ◽  
Alan B. Richards ◽  
...  
Cytokine ◽  
1994 ◽  
Vol 6 (5) ◽  
pp. 572
Author(s):  
R. Mock ◽  
J. Cummins ◽  
B. Shive ◽  
S. Krakowka ◽  
A. Richards ◽  
...  

Parasitology ◽  
1990 ◽  
Vol 101 (2) ◽  
pp. 201-209 ◽  
Author(s):  
A. S. Young ◽  
A. C. Maritim ◽  
D. P. Kariuki ◽  
D. A. Stagg ◽  
J. M. Wafula ◽  
...  

Two natural human interferon alpha preparations, (nHuIFN-μ [Cantell]) and (Nhuifn-μ [ISI]), were used for the oral treatment of cattle experimentally infected with Theileria parva parva. In the first experiment, 8 Friesian bulls were inoculated with a 1 in 10 dilution of a sporozoite stabilate of T. p. parva (Marikebuni) stock. Four of the cattle were treated daily with 1 international unit/kg body weight (i.u./kg bwt) of nHuIFN-μ (Cantell) from day –2 to day 8 p.i. None of the 4 calves given IFN developed clinical theileriosis, but 3 of the 4 control calves died of theileriosis while the fourth had a mild infection. Three of 4 treated calves and the 1 surviving control calf developed a detectable antibody response to T. p. parva schizont antigen but, on challenged with a 10-fold higher dose of stabilate, the surviving control animal and only 1 of the 4 treated calves proved to be immune. In a second experiment, 4 groups of 4 calves were inoculated with the same stabilate dilution. Three treatment groups were given either 1 i.u. nHuIFN-μ (Cantell), 1 i.u. nHuIFN-μ (ISI), or 10 i.u. nHuIFN-μ (ISI)/kg bwt from day –2 to day 8 p.i. once daily and the fourth group were controls. Clinical theileriosis occurred in 2 controls, 2 calves given 10 i.u. nHuINF-μ (ISI), 1 calf given 1 i.u. nHuIFN-μ (ISI) and no calves given 1 i.u. nHuIFN-μ (Cantell)/kg bwt. Of these, 2, 1, 0 and 0 cattle died in the respective groups. All the surviving cattle proved to be immune on homologous challenge with 10-fold higher dose of stabilate except the 2 cattle which did not develop high antibody responses. A third experiment using an undiluted challenge of T. p. parva (Muguga) sporozoite stabilate (10α) on 8 steers. Four steers were treated with 1 i.u. nHuIFN-α (Cantell)/kg bwt and 4 were controls. All calves developed acute theileriosis and the experiment was terminated. Cells of the C2 lymphoblastoid cell line, infected with T. p. parva (Muguga) schizonts, were cultured in vitro with various concentrations (0-01-100 i.u./ml) of nHuIFN-a (Cantell). The IFN appeared to have no effect on host cell or parasite developmental variables when compared to untreated control cultures.


1983 ◽  
Vol 3 (2) ◽  
pp. 231-239 ◽  
Author(s):  
I. HERON ◽  
M. HOKLAND ◽  
K. BERG

Biochimie ◽  
2010 ◽  
Vol 92 (8) ◽  
pp. 971-978 ◽  
Author(s):  
Natalia Ceaglio ◽  
Marina Etcheverrigaray ◽  
Ricardo Kratje ◽  
Marcos Oggero

Author(s):  
Christin Pohl ◽  
Marco Polimeni ◽  
Sowmya Indrakumar ◽  
Werner Streicher ◽  
Günther H.J. Peters ◽  
...  

2018 ◽  
Vol 22 (2) ◽  
pp. 57
Author(s):  
Ratih Asmana Ningrum ◽  
Widdya Kusuma Wardhani ◽  
Ike Wahyuni ◽  
Apon Zaenal Mustopa

     Recombinant Human Interferon Alpha-2a (rhIFNα-2a) is a therapeutic protein that used in hepatitis and cancer treatments. In our previous research, we developed higher molecular weight of the protein through human serum albumin fusion. The fusion and non fusion form of rhIFNα-2a were produced in Pichia pastoriswith 86 kDa and 19 kDa in size respectively. In previous research, protein yield was not reproducible due to unoptimized expression conditions. This reseach was aimed to optimize expression condition process and to characterize the fusion and non fusion forms of rhIFNα-2a. The parameters to observe in overproduction include nutrient (media and methanol concentration) and non nutrient (temperature andincubation period). Affinity and size exclusion cromatographicwere compared in protein purification. BCA assay was used to determine quantity of protein. Protein characterization was conducted using two-dimensional SDS PAGE and denaturation analyses. The optimal condition of expression was achieved using complex media with 1% of methanol for 3 day incubation period at 25°C. The protein yield was reproducible and higher comparing to previous research. Affinity chromatography resulted in higher purity of the proteins comparing to size exclusions. Characterization using two dimensional gel analysis revealed that isoelectric point of rhIFNα-2a is 6.5 for fusion form and 6.0 for non fusion form. The melting points of fusion protein were 56°C and 62°C whilst that of non fusion was 56°C.


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