Isolation of human nerve growth factor from placental tissue

L. D. Goldstein, C. P. Reynolds, J. R. Perez-Polo

    Research output: Contribution to journalArticle

    82 Citations (Scopus)

    Abstract

    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.

    Original languageEnglish (US)
    Pages (from-to)175-183
    Number of pages9
    JournalNeurochemical Research
    Volume3
    Issue number2
    DOIs
    StatePublished - Apr 1978

    Fingerprint

    Nerve Growth Factor
    Tissue
    Cotyledon
    Isoelectric Focusing
    Molecular Weight
    Molecular weight
    Bioactivity
    Proteins
    Assays
    Serum
    DEAE-Dextran
    Amnion
    Centrifugation
    Spinal Ganglia
    Chickens
    Embryonic Structures
    Immunoglobulin G
    Mothers
    Rabbits

    ASJC Scopus subject areas

    • Neuroscience(all)
    • Biochemistry

    Cite this

    Goldstein, L. D., Reynolds, C. P., & Perez-Polo, J. R. (1978). Isolation of human nerve growth factor from placental tissue. Neurochemical Research, 3(2), 175-183. https://doi.org/10.1007/BF00964058

    Isolation of human nerve growth factor from placental tissue. / Goldstein, L. D.; Reynolds, C. P.; Perez-Polo, J. R.

    In: Neurochemical Research, Vol. 3, No. 2, 04.1978, p. 175-183.

    Research output: Contribution to journalArticle

    Goldstein, LD, Reynolds, CP & Perez-Polo, JR 1978, 'Isolation of human nerve growth factor from placental tissue', Neurochemical Research, vol. 3, no. 2, pp. 175-183. https://doi.org/10.1007/BF00964058
    Goldstein, L. D. ; Reynolds, C. P. ; Perez-Polo, J. R. / Isolation of human nerve growth factor from placental tissue. In: Neurochemical Research. 1978 ; Vol. 3, No. 2. pp. 175-183.
    @article{1534dcc0778c401997388b9d01adf4d8,
    title = "Isolation of human nerve growth factor from placental tissue",
    abstract = "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.",
    author = "Goldstein, {L. D.} and Reynolds, {C. P.} and Perez-Polo, {J. R.}",
    year = "1978",
    month = "4",
    doi = "10.1007/BF00964058",
    language = "English (US)",
    volume = "3",
    pages = "175--183",
    journal = "Neurochemical Research",
    issn = "0364-3190",
    publisher = "Springer New York",
    number = "2",

    }

    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

    Y1 - 1978/4

    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

    VL - 3

    SP - 175

    EP - 183

    JO - Neurochemical Research

    JF - Neurochemical Research

    SN - 0364-3190

    IS - 2

    ER -