Phase IV group study of natural human interferon alpha (HLBI) on chronic myelogeneous leukaemia

Biotherapy ◽  
1993 ◽  
Vol 6 (2) ◽  
pp. 149-153
Author(s):  
Shigeru Arimori ◽  
Hideo Terada ◽  
Kazuo Hayami ◽  
Yoshitaka Aoyagi ◽  
Shigeki Motomura ◽  
...  
Keyword(s):  
Interferon Alpha ◽  
Human Interferon ◽  
Chronic Myelogeneous Leukaemia ◽  
Phase Iv

13 Native Human Interferon-Alpha Species Assessed for Immunoregulatory Properties

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

Influence of carbohydrates on the stability and structure of a hyperglycosylated human interferon alpha mutein

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

scholarly journals Electrostatics Drive Oligomerization and Aggregation of Human Interferon Alpha-2a

2021 ◽  
Author(s):  
Christin Pohl ◽  
Marco Polimeni ◽  
Sowmya Indrakumar ◽  
Werner Streicher ◽  
Günther H.J. Peters ◽  
...  
Keyword(s):  
Interferon Alpha ◽  
Human Interferon

scholarly journals Optimization of Expression Condition, Two Dimensional And Melting Point-Based Characterization of Recombinant Human Interferon Alpha-2a Fusion and Non Fusion Forms

2018 ◽  
Vol 22 (2) ◽  
pp. 57
Author(s):  
Ratih Asmana Ningrum ◽  
Widdya Kusuma Wardhani ◽  
Ike Wahyuni ◽  
Apon Zaenal Mustopa
Keyword(s):  
Interferon Alpha ◽  
Protein Characterization ◽  
Protein Yield ◽  
Size Exclusion ◽  
Human Interferon ◽  
Two Dimensional ◽  
Cancer Treatments ◽  
Sds Page ◽  
Bca Assay

     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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