Yn. Fang et al., Isolation and partial molecular characterization of heat-stable growth factor from human placenta, SCI CHINA C, 41(6), 1998, pp. 628-635
A heat-stable growth factor has been purified to homogeneity from human pla
centa. Purification procedure involved extraction with acidic medium, preci
pitation using ethanol, DE-52 ion-exchange chromatography, and reversed-pha
se HPLC. The purified preparation has been named human placental growth fac
tor-1 (HPGF-1), which simulates the proliferation of some cell lines, such
as human amniotic cell, mouse marrow tumor cell, and mouse fibroblast cell.
The growth factor has an approximate molecular weight of 1 900. It is a gl
ycopeptide which contains a polypeptide chain consisting of 10 amino acid r
esidues with molecular weight of 1 195. The N-terminal residue of the polyp
eptide chain part is phenylalanine. The molecular weight of non-peptide par
t is 682. The isoelectric point of the growth factor is pI 6.8.