TY - JOUR
T1 - Isolation of human nerve growth factor from placental tissue
AU - Goldstein, L. D.
AU - Reynolds, C. P.
AU - Perez-Polo, J. R.
PY - 1978/4/1
Y1 - 1978/4/1
N2 - Nerve growth factor (NGF) has been isolated from human placental tissue. Using the chicken embryo dorsal root ganglia assay, we determined levels of NGF activity for the amnion, placental cotyledons, cord serum, fetal serum, and maternal serum. The highest levels of NGF activity were measured in placental cotyledons. After homogenization and centrifugation of the placental cotyledons, the supernatant was sequentially chromatographed, at neutral pH, on Sephadex G-100, DEAE-11, and Sephadex G-150. A high-molecular-weight protein fraction (≈150,000), which contained all the biological activity, was isolated in this fashion. Analytical isoelectric focusing of this fraction revealed a basic protein component (pI 9.5) of the high-molecular-weight species. Assays for NGF activity of all protein components separated by analytical isoelectric focusing showed that NGF activity was associated only with the basic protein component. Correspondingly, preparative isoelectric focusing of the high-molecular-weight species yielded a basic protein with very high biological activity (1-3 ng per biological unit) that was immunochemically active against rabbit IgG made against mouse β-NGF.
AB - Nerve growth factor (NGF) has been isolated from human placental tissue. Using the chicken embryo dorsal root ganglia assay, we determined levels of NGF activity for the amnion, placental cotyledons, cord serum, fetal serum, and maternal serum. The highest levels of NGF activity were measured in placental cotyledons. After homogenization and centrifugation of the placental cotyledons, the supernatant was sequentially chromatographed, at neutral pH, on Sephadex G-100, DEAE-11, and Sephadex G-150. A high-molecular-weight protein fraction (≈150,000), which contained all the biological activity, was isolated in this fashion. Analytical isoelectric focusing of this fraction revealed a basic protein component (pI 9.5) of the high-molecular-weight species. Assays for NGF activity of all protein components separated by analytical isoelectric focusing showed that NGF activity was associated only with the basic protein component. Correspondingly, preparative isoelectric focusing of the high-molecular-weight species yielded a basic protein with very high biological activity (1-3 ng per biological unit) that was immunochemically active against rabbit IgG made against mouse β-NGF.
UR - http://www.scopus.com/inward/record.url?scp=0018238503&partnerID=8YFLogxK
UR - http://www.scopus.com/inward/citedby.url?scp=0018238503&partnerID=8YFLogxK
U2 - 10.1007/BF00964058
DO - 10.1007/BF00964058
M3 - Article
C2 - 566860
AN - SCOPUS:0018238503
SN - 0364-3190
VL - 3
SP - 175
EP - 183
JO - Neurochemical Research
JF - Neurochemical Research
IS - 2
ER -