Purification and characterization of immunoglobulin production stimulating factor derived from human B lymphoblastoid HO-323 cells.
An immunoglobulin (Ig) production stimulating factor (IPSF) for hybridomas was found in spent medium of the human B lymphoblastoid cell line, HO-323. The IPSF was purified by serial use of DEAE chromatography, ultrafiltration, gel filtration and HPLC-DEAE chromatography. Purified IPSF was estimated to be a 410 k macro molecule by gel filtration, and contained three types of isomers which were separated from each other by native polyacrylamide gel electrophoresis. All of the isomers were, however, assumed to have the same protein components by SDS polyacrylamide gel electrophoresis. The IPSF was effective for human-human and mouse-mouse hybridomas producing IgM, but not for IgG producers in the experimental condition used here. Human-human hybridoma HF10B4, cultured in IPSF-containing medium, produced 20 times more IgM than in IPSF-free medium under serum-free conditions. The IPSF showed very little proliferation stimulating activity on HF10B4 cells.
Toyoda
K
K
Biotechnology Research Laboratory, Tosoh Corporation, Kanagawa. Japan.
Sugahara
T
T
Inouye
K
K
Yamada
K
K
Shirahata
S
S
Murakami
H
H
D001685:Biological Factors / Q000302:isolation & purification* / Q000494:pharmacology; D002455:Cell Division / Q000187:drug effects; D002460:Cell Line; D003470:Culture Media; D004591:Electrophoresis, Polyacrylamide Gel; D006801:Humans; D006825:Hybridomas / Q000166:cytology / Q000276:immunology; D007075:Immunoglobulin M / Q000096:biosynthesis; D007136:Immunoglobulins / Q000096:biosynthesis*; D008970:Molecular Weight
D001685:Biological Factors; D003470:Culture Media; D007075:Immunoglobulin M; D007136:Immunoglobulins