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Discovery of a human erythroid differentiation factor (EDF) and its large‐scale production
Author(s) -
Tsuji T.,
Eto Y.,
Takano S.,
Takezawa M.,
Yokogawa Y.,
Shibai H.
Publication year - 1988
Publication title -
biotechnology and bioengineering
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.136
H-Index - 189
eISSN - 1097-0290
pISSN - 0006-3592
DOI - 10.1002/bit.260310708
Subject(s) - pronase , biochemistry , phorbol , cellular differentiation , chemistry , microbiology and biotechnology , biology , enzyme , trypsin , protein kinase c , gene
A novel human protein exhibiting erythroid differentiation activity was discovered in the culture fluids of phorbol ester‐stimulated human cells. The differentiation assay system involving Friend virus‐derived mouse leukemia cells was used. THP‐1 cells of myelomonocytic origin were typical producers. 4β‐Phorbol 12‐myristate 13‐acetate (PMA) was essential for inducible excretion of the erythroid differentiation factor (EDF). The factor was stable toward heat and pH (acidic or alkaline) but lost its activity on pronase treatment, which suggested its proteinous nature. After an optimization of the condition, production of EDF was performed on a 200‐L scale for purification of the protein.