The binding activity of recombinant human interferon alpha-2a to its receptor on FL cells.

[The binding activity of recombinant human interferon alpha-2a to its receptor on FL cells].

The Effect of Heat Shock on Production of Recombinant Human Interferon Alpha 2a (rhIFN α -2a) by Escherichia coli

Recombinant human interferon alpha 2a (rhIFN α -2a) production and cell growth were monitored in a set of genetically modified E. coli strains (MSD1519, MSD1520, MSD 1521, MSD 1522, MSD 1523) producing rhIFN α -2a. The growth was followed at OD 600 nm, changes in cell physiology were detected by pyrolysis mass spectrometry (PyMS) of cell biomass and recombinant protein production was determined...

the effect of heat shock on production of recombinant human interferon alpha 2a (rhifn α -2a) by escherichia coli

recombinant human interferon alpha 2a (rhifn α -2a) production and cell growth were monitored in a set of genetically modified e. coli strains (msd1519, msd1520, msd 1521, msd 1522, msd 1523) producing rhifn α -2a. the growth was followed at od 600 nm, changes in cell physiology were detected by pyrolysis mass spectrometry (pyms) of cell biomass and recombinant protein production was determined...

Biologic activity in a fragment of recombinant human interferon alpha.

To attempt to locate functionally important regions of the interferon (IFN) molecule, recombinant human IFN-alpha 2 was subjected to proteolytic digestion. The bacterial proteinase thermolysin produced two major complementary fragments, HuIFN-alpha 2-(1-110) and HuIFN-alpha 2-(111-153). After reduction with 2-mercaptoethanol and separation of the two major fragments on NaDodSO4/polyacrylamide g...

Study on the Effect of Solution Conditions on Heat Induced-Aggregation of Human Alpha Interferon

A major problem in the formulation of therapeutic proteins is the irreversible protein aggregation. Recombinant human interferon alpha2b (rhIFN2b) has poor stability and undergoes physical degradation. The aim of this study was to investigate the effect of solution conditions on the heat-induced aggregation of rhIFNα2b. The protein was incubated for 1 h at 40°C–70°C and for up to 240 h at 50C...