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Neurotrophic factor - Characterization and partial purificationRecent evidence suggests that neurotrophic activity is required for the normal proliferation and development of muscle cells. The present paper reports a study of the purification and characterization of a neurotrophic factor (NTF) from adult chicken ischiatic-peroneal nerves using two independent quantitative in vitro assay systems. The assays were performed by the measurement of the incorporation of tritiated thymidine or the sizes of single-cell clones by chick muscle cells grown in culture. The greatest amount of neutrotrophic activity is found to be extracted at a pH of 8; aqueous suspensions of the activity are stable to long-term storage at room temperature. The specific activity of the substance is doubled upon precipitation with ammonium sulfate or after gel filtration, and increase 4 to 5 fold after salt gradient elution from DEAE cellulose columns. The active fraction obtained after gel filtration and rechromatography on DEAE cellulose exhibits a 7 to 10-fold increase in specific activity. Electrophoresis of the most highly purified material yields a greatly concentrated band at around 80,000 daltons. Although NTF is purified almost 10-fold as indicated by the increase in specific activity, the maximum activity of the partially purified material is greatly reduced, possibly due to a requirement for a cofactor for the expression of maximum activity.
Document ID
19820032163
Acquisition Source
Legacy CDMS
Document Type
Reprint (Version printed in journal)
Authors
Popiela, H.
(NASA Ames Research Center Moffett Field, CA, United States)
Ellis, S.
(NASA Ames Research Center Biomedical Research Div., Moffett Field, CA, United States)
Date Acquired
August 10, 2013
Publication Date
January 1, 1981
Publication Information
Publication: Developmental Biology
Volume: 83
Subject Category
Life Sciences (General)
Accession Number
82A15698
Distribution Limits
Public
Copyright
Other

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