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Preparation and Characterization of Novel HDL-mimicking Nanoparticles for Nerve Growth Factor Encapsulation
Published on: May 22, 2017
Biochemical characterization of recombinant human nerve growth factor
C H Schmelzer1, L E Burton, W P Chan
1Genetech, Inc., South San Francisco, California 94080.
Journal of Neurochemistry
|November 1, 1992
Summary
Recombinant human nerve growth factor (rhNGF) was purified and characterized. This protein dimer functions identically to its modified forms in cell survival and neurite extension assays.
Area of Science:
- Biochemistry
- Molecular Biology
- Neuroscience
Background:
- Nerve growth factor (NGF) is crucial for neuronal development and survival.
- Production of recombinant human NGF (rhNGF) is essential for therapeutic applications.
Purpose of the Study:
- To express, purify, and characterize recombinant human nerve growth factor (rhNGF).
- To assess the biological activity of purified rhNGF and its modified forms.
Main Methods:
- rhNGF expression in Chinese hamster ovary cells.
- Purification using ion-exchange and reversed-phase chromatography.
- Characterization via SDS-PAGE, HPLC, mass spectrometry, and enzymatic digestion.
Main Results:
- Purified rhNGF is a 120-amino acid polypeptide, existing as a noncovalent dimer.
- Enzymatic digestion yielded smaller rhNGF species (118 and 117 residues).
- All rhNGF forms (dimer, modified species) demonstrated equipotent biological activity in cell survival and neurite extension assays.
Conclusions:
- The study successfully produced and characterized functional rhNGF.
- rhNGF's biological activity is retained even after C-terminal modifications.
- These findings support the therapeutic potential of rhNGF.
