PRODUCTION AND PURIFICATION OF A FUSED RECOMBINANT RECOMBINANT PROTEIN GP-36 (HIV-2) FROM ESCHERICHIA-COLI

A fragment of the gp-36 gene of the Human Immunodeficiency Virus type 2 (HIV-2) was fused to a stabilizer sequence, which encodes for the fi rst N-terminal 58 amino acids of the human interleukin-2. The fused pr otein was expressed under the control of the tryptophan promoter in Es cherichia coli, and expressed as 20% of the total cellular protein. Tr ansmission electron microscopy indicated that the fusion protein forme d cytoplasmic insoluble inclusion bodies. Inclusion bodies were semipu rified by a wash pellet cell procedure, rendering a material with a pu rity higher than 70% by SDS-polyacrylamide gel electrophoresis. After solubilization with urea, this preparation was further purified by gel -filtration chromatography up to 95% purity.