Recombinant human nerve growth factor (rhNGF) secreted by insect cells was purified by ion‐exchange and reversed‐phase chromatography to near homogeneity. The Nterminus of the secreted molecule was analogous to that of mouse salivary gland NGF. In its native conformation, the insect cell produced rhNGF molecules were homodimers consisting of 120 amino acid polypeptide chains. Mature rhNGF was found not to be significantly glycosylated (<0.08 mol of N‐acetylglucosamine/mol of protein). The rhNGF was homogeneous with regard to molecular weight and amino acid sequence. Isoelectric focusing resolved the rhNGF into one major and one minor component. Because rhNGF frominsect cells can be obtained in large quantities, purified to near homogeneity, and is similar to natural NGF with regard to physicochemical properties and biological activity, it is suitable for further evaluation in animal models as a therapeutic molecule for neurodegenerative diseases such as Alzheimer's disease.
|Number of pages||10|
|Journal||Journal of Neurochemistry|
|State||Published - Sep 1991|
- Alzheimer's disease
- Nerve growth factor