S. Cholin et al., EXPRESSION OF A RECOMBINANT HUMAN GROWTH-HORMONE BINDING-PROTEIN IN BACULOVIRUS INSECT CELL SYSTEM/, Biochimie, 78(10), 1996, pp. 882-886
An eucaryotic recombinant human growth hormone binding protein (rGHBP)
was expressed in baculovirus-infected insect cells and purified by af
finity chromatography from culture supernatant. This mannose-rich 34-k
Da protein specifically bound human growth hormone (hGH) with the same
affinity (kDa = 0.42 x 10(-9) M) than the 51.5 kDa GHBP we purified a
nd characterised from human plasma (kDa = 1.1 x 10(-9) M). A high mole
cular form of the rGHBP was detected by silver-stained SDS-PAGE, Weste
rn blot (mAb 263), affinity cross-linking and Western ligand blot with
I-125-hGH. Reduction experiments with beta-mercaptoethanol suggested
that this form involved a disulfide bound between two rGHBPs.