title: The nerve growth factor: purification as a 30,000-molecular-weight protein.
abstract: The nerve growth factor protein was purified over 100-fold from adult mouse salivary glands. The first step was a gel filtration on Sephadex G-100 at pH 7.5 of the aqueous gland extract. After gel filtration, most of the NGF activity was eluted in the 80,000-90,000-molecular-weight region (G-100 pool). The G-100 pool was dialyzed at pH 5.0 and fractionated by CM52 cellulose chromatography at pH 5.0. Recovery from CM52 cellulose columns was quantitative for protein and ranged 80-100 per cent for the nerve growth factor activity; the latter was almost completely carried by a protein which did not show any heterogeneity when examined by several analytical tests. The purified nerve growth factor showed an S(20,w) = 2.43, a D(20,w) = 7.30 and a 30,000 molecular weight. The over-all recovery was about 45 per cent.
mesh_terms: D000818:Animals; D000831:Animals, Newborn; D001681:Biological Assay; D002850:Chromatography, Gel; D003956:Dialysis; D004589:Electrophoresis, Disc; D006133:Growth Substances / Q000302:isolation & purification*; D005779:Immunodiffusion; D051379:Mice; D008970:Molecular Weight; D009414:Nerve Growth Factors / Q000302:isolation & purification; D011506:Proteins / Q000302:isolation & purification*; D013363:Submandibular Gland / Q000032:analysis*; D014461:Ultracentrifugation
chemical_list: D006133:Growth Substances; D009414:Nerve Growth Factors; D011506:Proteins